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CDS information : Chro_00190


close this sectionLocation

Organism
StrainATCC 13273 (=NBRC 3746)
Entry nameChromomycin
Contig
Start / Stop / Direction19,818 / 21,338 / + [in whole cluster]
19,818 / 21,338 / + [in contig]
Location19818..21338 [in whole cluster]
19818..21338 [in contig]
TypeCDS
Length1,521 bp (506 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category3.3 modification reduction
ProductBaeyer-Villiger monooxygenase
Product (GenBank)oxygenase
Gene
Gene (GenBank)cmmOIV
EC number
Keyword
  • ring opening
Note
Note (GenBank)
Reference
ACC
PmId
[15112992] Biosynthesis of the antitumor chromomycin A3 in Streptomyces griseus: analysis of the gene cluster and rational design of novel chromomycin analogs. (Chem Biol. , 2004)
[21244022] Characterization of the terminal activation step catalyzed by oxygenase CmmOIV of the chromomycin biosynthetic pathway from Streptomyces griseus. (Biochemistry. , 2011)
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)

close this sectionSequence

selected fasta
>Baeyer-Villiger monooxygenase [oxygenase]
MEYDVVVAGSGPVGLTLACELRLAGVRVLVVDRLTEPAGHDRAGVLHTRTVECLDIRGLL
DRFEDGADTVSGLPFAGIFSKGLDHGTLDTGHPYSLLVPQSRTEELLAARAAELGVPIRR
GHEVVALRQDPDGVSVGIRTADGHHEVRARYLVGCDGGRSTVRRLAGIPFPGFPASVSAM
IGYVTLPEKDVPRRWQRTPAGVAVLAFPSEGGTGRVVVIEYGREHPSPQDPVTLEELRAG
VRRVYGRELGLTEPVAWMSRFSDATRQAERYRSGRVLLAGDAAHIHFPIGGQGLNTGVHD
AMNLGWKLAAEIGGWAPEGLLDSYHEERHRAGARVLTYTRAQLALMNPDEHHVTALREVF
EELLGLQDTNRLLTAALNGVDVRYGGTAEEGGPPDGGDGPEPRHPLDGLFAPDLVLEGGQ
GSGRLAELLHTGRGVLLDLTEGGTPAKAARPWEHRIDVVRARCPAGAPAAALLVRPDGHV
AWAADDGTERGLRDALARWFGSQDGR
selected fasta
>Baeyer-Villiger monooxygenase [oxygenase]
ATGGAGTACGACGTCGTCGTGGCGGGCAGCGGGCCGGTCGGCCTGACGCTCGCCTGCGAA
CTGCGGCTGGCCGGTGTCCGGGTGCTGGTGGTCGACCGGCTCACGGAACCGGCGGGCCAC
GACCGGGCCGGCGTGCTGCACACCCGCACGGTGGAATGCCTGGACATCCGCGGACTGCTG
GACCGGTTCGAGGACGGGGCCGACACGGTGTCCGGGCTGCCGTTCGCCGGGATCTTCAGC
AAGGGGCTCGACCACGGGACGCTCGACACCGGGCATCCGTACAGTCTCTTGGTCCCCCAG
TCGCGTACCGAGGAACTGCTCGCCGCCCGTGCGGCCGAACTCGGCGTGCCGATCCGGCGC
GGGCACGAGGTCGTCGCGCTGCGCCAGGACCCCGACGGGGTGAGCGTCGGTATCCGCACC
GCGGACGGCCACCATGAGGTGCGTGCCCGCTACCTGGTGGGGTGCGACGGAGGGCGCAGC
ACGGTGCGCCGCCTCGCGGGCATCCCCTTCCCCGGCTTCCCCGCCTCGGTGAGCGCCATG
ATCGGTTACGTCACACTTCCGGAGAAGGACGTTCCCCGCCGCTGGCAGAGGACCCCGGCC
GGCGTGGCGGTGCTCGCCTTCCCCTCGGAGGGCGGAACGGGCCGTGTGGTGGTCATCGAG
TACGGCCGTGAGCATCCGTCCCCGCAGGACCCGGTGACCCTGGAGGAGCTGCGGGCCGGC
GTCCGCCGGGTGTACGGACGGGAACTCGGCCTCACGGAACCGGTGGCGTGGATGTCCCGG
TTCAGCGACGCCACCCGGCAGGCCGAGCGGTACCGCTCCGGGCGGGTCCTCCTCGCCGGG
GACGCCGCCCACATCCACTTCCCGATCGGCGGGCAGGGCCTCAACACCGGCGTTCACGAC
GCCATGAACCTCGGCTGGAAGCTCGCGGCGGAGATCGGCGGATGGGCACCGGAGGGACTC
CTCGACTCGTACCACGAGGAACGCCACCGGGCCGGGGCGCGGGTGCTGACGTACACCCGC
GCCCAGCTCGCGCTGATGAACCCGGACGAGCACCATGTGACCGCCCTGCGGGAGGTCTTC
GAGGAACTGCTCGGGCTTCAGGACACCAACCGGCTCCTGACCGCCGCCCTCAACGGAGTC
GACGTCCGGTACGGAGGTACGGCGGAGGAGGGCGGGCCACCGGACGGCGGAGACGGTCCG
GAGCCACGGCACCCGCTGGACGGACTGTTCGCCCCGGACCTCGTCCTTGAAGGCGGGCAG
GGGAGCGGCCGCCTGGCGGAACTGCTGCACACGGGACGCGGCGTGCTCCTCGACCTGACC
GAGGGCGGGACACCGGCCAAGGCCGCCCGTCCCTGGGAGCACCGCATCGACGTGGTCCGG
GCGCGATGCCCTGCGGGAGCGCCCGCCGCGGCGCTGCTCGTGCGGCCCGACGGCCATGTG
GCCTGGGCGGCGGACGACGGGACCGAGCGCGGGCTGCGCGATGCGCTGGCCCGGTGGTTC
GGGTCCCAGGACGGGAGGTAG

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09
show BLAST table
InterPro
Database:interpro:38.0
IPR002938 Monooxygenase, FAD-binding (Domain)
 [2-337]  2.59999999999995e-86 PF01494
PF01494   FAD_binding_3
IPR003042 Aromatic-ring hydroxylase-like (Domain)
 [4-26]  2.50000909916183e-42 PR00420 [148-163]  2.50000909916183e-42 PR00420 [273-288]  2.50000909916183e-42 PR00420 [288-304]  2.50000909916183e-42 PR00420 [306-324]  2.50000909916183e-42 PR00420 [324-340]  2.50000909916183e-42 PR00420
PR00420   RNGMNOXGNASE
SignalP No significant hit
TMHMM No significant hit