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CDS information : Polk_00390


close this sectionLocation

Organism
StrainTü6028
Entry namePolyketomycin
Contig
Start / Stop / Direction47,306 / 48,826 / + [in whole cluster]
47,306 / 48,826 / + [in contig]
Location47306..48826 [in whole cluster]
47306..48826 [in contig]
TypeCDS
Length1,521 bp (506 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category3.3 modification reduction
Productputative oxidoreductase
Product (GenBank)PokO4
Gene
Gene (GenBank)pokO4
EC number
Keyword
Note
Note (GenBank)
  • putative monooxygenase
Reference
ACC
PmId
[19266534] Organisation of the biosynthetic gene cluster and tailoring enzymes in the biosynthesis of the tetracyclic quinone glycoside antibiotic polyketomycin. (Chembiochem. , 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
Q8KSX5
NITE
Griseo_00170
PmId
[19175308] Cleavage of four carbon-carbon bonds during biosynthesis of the griseorhodin a spiroketal pharmacophore. (J Am Chem Soc. , 2009)
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 [PokO4]
MNTDVVVVGGGPVGLLLAAELRLGGARVVLLERLTEPSGHSRAFRMQARMLDVLDQRGLL
DRFKEGNRTWPKAHFAGLEPLLDFGHLRNEHPYALLIPQARTEELLEEHALACGVEIRRG
HTLRGLDATPSDVVAEVESPEGTYRLRSHYLVGCDGGRSTVRKLAGIGFGGSPPTVRALL
ADVELADPGQLPNGVPGTMRTPRGLLMAISLQPGVTRVLTTEFTPPEPGSEHAPVTLDEL
RETVRRITGIDVAMDRPRWLSRFADTTRLADTYRQGRVLLAGDAAHVHFPIGAQGLNLGL
QDAVNLGWKLAGTIVGWAPPGLLDSYGSERRPVAGRVLRETRVQLLLMAPDPKVDPLREM
FAELLALPEVNSRLAHEMTGLDVHYAAAAGRYEHGLLGRPCPPLPASVGDEVRTVLRTGR
GALLLPEGPAEEAARLATEWSHRVGRVATEDGQGLLLRPDGHVAWVDPGDGVPRKDVLLE
LEDALRRWFGAPGCTVLSRNDDTAGR
selected fasta
>putative oxidoreductase [PokO4]
ATGAACACCGACGTCGTCGTGGTCGGAGGGGGCCCGGTCGGTCTGCTGCTCGCCGCCGAA
CTGCGGCTCGGGGGCGCCCGCGTGGTCCTCCTGGAGCGGCTGACGGAGCCGAGCGGGCAC
TCCCGGGCCTTCCGCATGCAGGCGAGGATGCTGGACGTCCTGGACCAGCGAGGCCTGCTC
GACCGGTTCAAGGAGGGCAACCGGACCTGGCCGAAAGCCCATTTCGCGGGCCTGGAACCG
TTGCTCGACTTCGGGCACCTGCGCAACGAGCACCCCTACGCCCTGCTCATCCCGCAGGCG
CGCACCGAGGAGCTCCTGGAGGAGCACGCCCTGGCGTGCGGAGTCGAGATCCGCCGCGGG
CACACGCTCCGGGGGCTCGACGCCACGCCCTCCGACGTCGTGGCCGAGGTCGAGTCGCCC
GAGGGCACCTACCGGTTGCGCTCCCACTACCTGGTCGGCTGCGACGGCGGTCGCAGCACC
GTCCGCAAGCTCGCGGGCATCGGTTTCGGCGGCTCGCCGCCCACGGTCCGGGCGCTCCTC
GCCGACGTGGAACTGGCCGACCCCGGACAGCTGCCCAACGGAGTGCCGGGCACCATGCGC
ACCCCCCGGGGTCTGCTGATGGCGATCTCCCTGCAACCCGGCGTGACCCGGGTGCTCACC
ACCGAGTTCACCCCGCCGGAGCCCGGCTCCGAGCACGCGCCGGTGACCCTGGACGAACTG
CGCGAGACGGTGCGCAGGATCACCGGCATCGACGTCGCGATGGACCGGCCGCGCTGGCTG
TCCCGGTTCGCCGACACGACCCGGCTGGCGGACACCTACCGGCAGGGCCGCGTGCTGCTC
GCCGGCGACGCGGCCCACGTGCACTTCCCCATAGGAGCGCAGGGCCTCAACCTCGGCCTC
CAGGACGCCGTGAACCTCGGCTGGAAGCTGGCCGGGACCATCGTCGGATGGGCGCCGCCC
GGACTGCTCGACAGCTACGGCTCCGAGCGCCGCCCGGTCGCCGGGCGCGTGCTGCGCGAG
ACCCGGGTGCAGCTCCTGCTCATGGCCCCCGACCCCAAGGTCGACCCGCTCCGCGAGATG
TTCGCGGAGCTTCTCGCGCTCCCCGAGGTCAACAGCCGTCTCGCGCACGAGATGACAGGC
CTGGACGTCCACTACGCCGCCGCCGCGGGCCGCTACGAGCACGGCCTGCTCGGCCGCCCC
TGCCCTCCGCTGCCGGCCTCGGTCGGTGACGAGGTCCGCACGGTCCTGCGCACGGGCCGC
GGGGCACTGCTCCTGCCGGAGGGCCCGGCCGAGGAGGCCGCGCGGCTCGCCACCGAGTGG
TCGCACCGCGTCGGCCGGGTCGCGACCGAGGACGGACAGGGCCTGCTGCTCCGACCCGAC
GGCCATGTCGCGTGGGTGGACCCCGGCGACGGGGTGCCCCGCAAGGACGTGCTGCTGGAG
CTGGAGGACGCCCTGCGGCGCTGGTTCGGCGCTCCCGGCTGCACGGTCCTGTCCCGCAAC
GACGACACGGCCGGCAGGTGA

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09
show BLAST table
InterPro
Database:interpro:38.0
IPR002938 Monooxygenase, FAD-binding (Domain)
 [3-340]  5.69999999999998e-80 PF01494
PF01494   FAD_binding_3
IPR003042 Aromatic-ring hydroxylase-like (Domain)
 [4-26]  1.3000049540733e-42 PR00420 [147-162]  1.3000049540733e-42 PR00420 [275-290]  1.3000049540733e-42 PR00420 [290-306]  1.3000049540733e-42 PR00420 [308-326]  1.3000049540733e-42 PR00420 [326-342]  1.3000049540733e-42 PR00420
PR00420   RNGMNOXGNASE
SignalP
 [1-26]  0.421 Signal
Eukaryota   
TMHMM No significant hit