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CDS information : Chth_00330


close this sectionLocation

Organism
StrainDSM 40725
Entry nameChlorothricin
Contig
Start / Stop / Direction98,302 / 99,798 / + [in whole cluster]
98,302 / 99,798 / + [in contig]
Location98302..99798 [in whole cluster]
98302..99798 [in contig]
TypeCDS
Length1,497 bp (498 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category3.3 modification reduction
Productputative oxidoreductase
Product (GenBank)ChlE3
Gene
Gene (GenBank)chlE3
EC number
Keyword
Note
Note (GenBank)
  • FAD-dependent oxygenase
Reference
ACC
PmId
[16793515] Genetic characterization of the chlorothricin gene cluster as a model for spirotetronate antibiotic biosynthesis. (Chem Biol. , 2006)
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 [ChlE3]
MNHSVVVVGAGPVGLMLAAELARAGVPTLVLERRAETGERAPGLAINSAVVELFAQRGIM
DSLQGDGMEFPRAHFAHIWLDPAALAGEHPYTFLVPHHRVAQRLEDHATKAGAQVRRGAE
VIGLRQDASGAELDVRWDGGTEVIRAAYVVGCDGAGSAVRRLAGIGFPGVDEVFYGLVGD
LSVEAGDPLFDRLGVHQHDDGFFTVGPVSQNVLRVTTGEFDAAPGDPDAEVTGEELAAHV
RRLTGAELTTRGTPRWLSRWTAATRQAERYREGRVFLAGDAAHVHFPLGGQALSTGIEDA
VNLGWKLAASLADLAPAGLLDTYHEERHPVGARACSTTRAQMTLLRPGSGTGPLRELLTE
LVGLGEVNDHLVSLVGGLDIRYASLAGEGAHTLAGRRLPVTEVATDGGPVSVSEVAHSGR
GVLLDLSPGGGLAATVAAAWRERIDMVSGAPVKGLPEGVLLRPDGRVAWAGTAADGTGLT
EAAARWFGPGTAGRDRRD
selected fasta
>putative oxidoreductase [ChlE3]
ATGAACCACTCCGTCGTAGTCGTCGGCGCGGGCCCCGTGGGCCTCATGCTGGCCGCCGAG
CTGGCCCGGGCGGGCGTACCGACGCTGGTGCTCGAACGCAGGGCGGAGACCGGGGAGCGG
GCCCCCGGCCTGGCGATCAACTCCGCCGTCGTCGAACTGTTCGCCCAGCGCGGGATCATG
GACAGCCTGCAGGGCGACGGCATGGAGTTCCCGCGAGCCCACTTCGCTCATATCTGGCTC
GACCCCGCCGCGCTCGCCGGGGAGCACCCGTACACCTTTTTGGTGCCGCACCACCGGGTG
GCGCAGCGGCTGGAGGACCATGCGACGAAGGCGGGGGCGCAGGTACGGCGCGGCGCCGAG
GTGATCGGCCTGCGCCAGGACGCCTCCGGTGCCGAGCTCGACGTCCGGTGGGACGGCGGG
ACCGAAGTGATCCGCGCCGCGTACGTGGTGGGCTGCGACGGCGCGGGCAGCGCGGTGCGC
AGGCTGGCCGGGATCGGCTTCCCCGGTGTCGACGAGGTCTTCTACGGGCTCGTCGGGGAC
CTGAGCGTCGAGGCGGGCGATCCGCTGTTCGACCGGCTCGGGGTGCACCAGCACGACGAC
GGGTTCTTCACGGTGGGGCCGGTGTCGCAGAACGTGCTGCGGGTGACGACCGGGGAGTTC
GACGCGGCACCGGGCGACCCCGACGCCGAGGTCACCGGGGAGGAACTCGCCGCGCACGTA
CGACGGTTGACGGGTGCCGAACTGACCACGCGGGGCACGCCCCGCTGGCTGTCGCGCTGG
ACCGCCGCCACCCGGCAGGCCGAACGCTACCGGGAAGGCCGGGTGTTCCTCGCCGGCGAC
GCCGCGCATGTGCACTTCCCGCTGGGCGGACAGGCGTTGAGCACCGGCATCGAGGACGCG
GTCAACCTCGGCTGGAAGCTGGCCGCGAGCCTTGCGGACCTGGCCCCCGCAGGGCTGCTC
GACACCTACCACGAGGAGCGGCACCCGGTGGGCGCCCGCGCCTGCTCCACGACGCGGGCG
CAGATGACGCTGCTGCGGCCCGGCAGCGGGACGGGCCCCCTGCGGGAGCTGCTGACCGAA
CTGGTGGGACTCGGCGAGGTCAACGACCATCTCGTGTCGCTGGTGGGCGGCCTCGACATC
CGCTACGCGTCCCTCGCCGGGGAAGGCGCCCACACCCTGGCAGGGCGCAGGCTTCCGGTG
ACCGAGGTGGCGACGGACGGCGGACCGGTCTCCGTCAGCGAGGTGGCGCACTCCGGGCGG
GGCGTGCTGCTCGATCTGTCGCCGGGCGGTGGGCTCGCCGCGACCGTGGCTGCGGCATGG
CGTGAGCGGATCGACATGGTGAGCGGTGCGCCCGTGAAGGGCCTTCCGGAGGGGGTCCTG
CTGCGGCCGGACGGCCGTGTCGCCTGGGCGGGGACGGCCGCCGACGGGACGGGGCTGACC
GAGGCCGCCGCGCGGTGGTTCGGCCCGGGGACGGCCGGGCGGGACCGACGGGACTGA

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09
show BLAST table
InterPro
Database:interpro:38.0
IPR002938 Monooxygenase, FAD-binding (Domain)
 [4-335]  3.30000000000002e-75 PF01494
PF01494   FAD_binding_3
IPR003042 Aromatic-ring hydroxylase-like (Domain)
 [4-26]  6.10002656149838e-41 PR00420 [145-160]  6.10002656149838e-41 PR00420 [272-287]  6.10002656149838e-41 PR00420 [287-303]  6.10002656149838e-41 PR00420 [305-323]  6.10002656149838e-41 PR00420 [323-339]  6.10002656149838e-41 PR00420
PR00420   RNGMNOXGNASE
SignalP
 [1-24]  0.946 Signal
Eukaryota   
 [1-24]  0.972 Signal
Bacteria, Gram-positive   
 [1-24]  0.904 Signal
Bacteria, Gram-negative   
TMHMM No significant hit