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CDS information : Chth_00250


close this sectionLocation

Organism
StrainDSM 40725
Entry nameChlorothricin
Contig
Start / Stop / Direction29,807 / 31,357 / + [in whole cluster]
29,807 / 31,357 / + [in contig]
Location29807..31357 [in whole cluster]
29807..31357 [in contig]
TypeCDS
Length1,551 bp (516 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category3.3 modification reduction
Productputative oxidoreductase
Product (GenBank)ChlE1
Gene
Gene (GenBank)chlE1
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 [ChlE1]
MTSDVVVVGGGPTGLMLAYELALAGVRPLVLEQQSEPRTEPKANGLVGRIVQLLDYRGLL
DRFAEGSRHVGPAPSFYFGAVPLNLSALEHNPLHLLVIPQPRLETLLAESAVALGAEIRR
GQRVVALSQDDEGVTLETQGPDGNEALRAAYVVGCDGAHSTVRKQAGIGFPGSTGSLVTR
IGHVSLPASLLVPETGEAEVPGAGRLRLGWTYTERGKIGLMSFKPGVHVVTAAENDRLPV
DSGAPMTLGELRSSVRRILGADLPMSNPLWLSRTVASSRLADRYRVGRVMVAGDAAHLFP
AGGSALNTGMLDAVNLGWKLAAQVTGTAPDGLLETYHDERHTVGEQVLAHTRAQAVLMAV
GEEPAVLRDLFEEVLRLPQAIRHIAERLHGEDVRYGAGALGDGAHPLLGRWAPDLALRTT
QGPARVAELLHAGRPVLLDLGGGGAALHDIVTEGWKDRVDVVAACAEQPAPPADALLIRP
DGHVAWAMPPARPTQEVREGLRAALTTWFGAPAKAL
selected fasta
>putative oxidoreductase [ChlE1]
ATGACTTCAGACGTCGTGGTGGTCGGCGGTGGCCCGACGGGGCTGATGCTGGCCTACGAA
CTCGCCCTGGCCGGAGTGCGCCCCCTCGTCCTCGAACAGCAGAGCGAGCCACGGACCGAG
CCCAAGGCGAACGGGCTGGTCGGCCGGATCGTCCAACTGCTGGACTACCGGGGCCTGCTC
GACCGGTTCGCCGAGGGGTCCCGGCATGTGGGCCCGGCCCCCTCGTTCTACTTCGGGGCG
GTCCCCCTGAACCTGTCCGCCCTGGAGCACAATCCGCTGCATCTGCTGGTGATCCCGCAA
CCCCGGCTGGAGACCCTGCTGGCGGAGAGCGCGGTCGCGCTGGGCGCCGAGATCCGCCGC
GGGCAACGCGTGGTGGCCCTGTCGCAGGACGACGAGGGGGTGACCCTGGAGACCCAGGGC
CCCGACGGCAACGAGGCGCTGCGCGCCGCCTACGTGGTGGGCTGCGACGGGGCGCACAGC
ACCGTGCGCAAACAGGCGGGCATCGGCTTCCCGGGCTCCACCGGCTCGCTGGTGACCCGG
ATCGGCCATGTCTCCCTGCCCGCCTCGCTGCTCGTGCCGGAGACCGGGGAGGCGGAGGTG
CCGGGCGCGGGACGGCTGCGGCTCGGCTGGACGTACACGGAGCGCGGGAAGATCGGGCTG
ATGTCCTTCAAGCCCGGGGTGCATGTGGTGACGGCGGCCGAGAACGACCGGCTGCCCGTG
GACTCCGGCGCGCCCATGACGCTCGGTGAGCTGCGCTCCAGCGTCCGCCGGATCCTGGGC
GCGGACCTGCCGATGAGCAACCCGCTGTGGCTGTCGCGGACGGTGGCCAGCAGCCGGCTG
GCCGACCGCTACCGGGTGGGCCGGGTCATGGTGGCCGGTGACGCGGCCCATCTGTTCCCG
GCGGGCGGTTCGGCGCTCAACACCGGGATGCTCGACGCGGTGAACCTGGGCTGGAAGCTG
GCCGCGCAGGTGACCGGCACGGCACCGGACGGCCTGCTGGAGACGTACCACGACGAGCGG
CACACCGTGGGCGAGCAGGTCCTGGCCCACACCCGGGCGCAGGCCGTCCTGATGGCCGTA
GGGGAGGAGCCCGCCGTCCTGCGCGACCTCTTCGAGGAGGTGCTGCGGCTGCCCCAGGCG
ATCCGGCACATCGCGGAGCGGCTGCACGGCGAGGACGTACGGTACGGGGCCGGCGCGCTC
GGCGACGGGGCGCATCCGCTGCTCGGGCGATGGGCGCCCGACCTCGCGCTGCGGACCACA
CAGGGGCCGGCCCGGGTCGCCGAACTGCTGCACGCGGGGCGGCCGGTACTGCTCGACCTC
GGGGGCGGCGGGGCGGCTCTGCACGACATCGTGACCGAGGGCTGGAAGGACCGCGTGGAC
GTGGTGGCCGCGTGCGCCGAACAGCCCGCTCCCCCGGCCGACGCCCTGCTGATCCGGCCC
GACGGTCATGTGGCGTGGGCGATGCCCCCGGCGCGGCCGACGCAGGAGGTGCGCGAGGGG
CTGCGCGCCGCGCTGACCACCTGGTTCGGGGCCCCCGCGAAGGCGCTCTAG

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09
show BLAST table
InterPro
Database:interpro:38.0
IPR002938 Monooxygenase, FAD-binding (Domain)
 [3-349]  1.29999999999998e-71 PF01494
PF01494   FAD_binding_3
IPR003042 Aromatic-ring hydroxylase-like (Domain)
 [4-26]  7.30000590915205e-34 PR00420 [148-163]  7.30000590915205e-34 PR00420 [286-301]  7.30000590915205e-34 PR00420 [318-336]  7.30000590915205e-34 PR00420 [336-352]  7.30000590915205e-34 PR00420
PR00420   RNGMNOXGNASE
SignalP
 [1-24]  0.226 Signal
Bacteria, Gram-negative   
TMHMM No significant hit