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CDS information : Ovied_00160


close this sectionLocation

Organism
StrainATCC 11891
Entry nameOviedomycin
Contig
Start / Stop / Direction14,453 / 15,925 / + [in whole cluster]
14,453 / 15,925 / + [in contig]
Location14453..15925 [in whole cluster]
14453..15925 [in contig]
TypeCDS
Length1,473 bp (490 aa)
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close this sectionAnnotation

Category3.4 other modification
Product2,3-dehydratase
Product (GenBank)oxygenase
Gene
Gene (GenBank)ovmOII
EC number
Keyword
Note
  • It is proposed that this ORF also serves as key enzyme bridging PKS and post-PKS reactions by catalyzing the hydrolysis and decarboxylation of the ACP-tethered angucycline to prejadomycin(2,3-dehydro-UWM6).
Note (GenBank)
Reference
ACC
PmId
[15368568] Genetic organization of the biosynthetic gene cluster for the antitumor angucycline oviedomycin in Streptomyces antibioticus ATCC 11891. (Chembiochem. , 2004)
[18988223] Elucidation of oxygenation steps during oviedomycin biosynthesis and generation of derivatives with increased antitumor activity. (Chembiochem. , 2009)
Related Reference
ACC
Q6DV92
NITE
Lando_00080
PmId
[15651811] Identification of the function of gene lndM2 encoding a bifunctional oxygenase-reductase involved in the biosynthesis of the antitumor antibiotic landomycin E by Streptomyces globisporus 1912 supports the originally assigned structure for landomycinone. (J Org Chem. , 2005)
[22454092] Elucidation of post-PKS tailoring steps involved in landomycin biosynthesis. (Org Biomol Chem. , 2012)
ACC
Q5U915
NITE
Jado_00130
PmId
[15817470] Functional analyses of oxygenases in jadomycin biosynthesis and identification of JadH as a bifunctional oxygenase/dehydrase. (J Biol Chem. , 2005)
[15776503] The oxidative ring cleavage in jadomycin biosynthesis: a multistep oxygenation cascade in a biosynthetic black box. (Chembiochem. , 2005)
[17346045] Multi-oxygenase complexes of the gilvocarcin and jadomycin biosyntheses. (J Am Chem Soc. , 2007)
[22465094] Delineation of gilvocarcin, jadomycin, and landomycin pathways through combinatorial biosynthetic enzymology. (Curr Opin Chem Biol. , 2012)

close this sectionSequence

selected fasta
>2,3-dehydratase [oxygenase]
MRTDVLVVGAGPVGLMLAGELRLGGAEVVVLDRLPRPTTESRATTLHARTMEILAARGLL
EALGTPPNDVMGHFGGVPLDLTLPTPYPGQWKVPQTRTEELLQAWALSLGATVRRGHELR
ALTVTDTGAEAEATGPDGRPVRVSARYVVGCDGERSTVRELTGADFPGQDATRELIRADV
AGIDIPDRRFQRLQRGLAIAARRPDGVTRVMVHEFGRAARPRTGAPAFAEVVDVWKRVTG
EDIGGGTPLWLNAFGDASRQVARYRDGRVLFAGDAAHVQMPVGGQALNLGLQDAVNLGWK
LAAEIRGRAPDGLLDTYHSERHAVGERVLSTIRAQSTFLLGGPDVEALREVFRELIDPAH
TRHTRAHLAGLISGLDIRYDVGPGDHPLLGARMPYGELDQAPDAACRKARGVLLDLAPGS
PSAAELHAVAAGWADRVDVVTAGFRTADGPSALSGARAVLVRPDGHVVWTDSGAGRPETA
LRRWFGAPVS
selected fasta
>2,3-dehydratase [oxygenase]
ATGCGGACTGACGTCCTCGTCGTCGGCGCGGGCCCGGTCGGGCTGATGCTCGCCGGTGAA
CTGCGCCTCGGCGGCGCCGAGGTGGTCGTGCTGGATCGGCTGCCCCGGCCCACCACCGAG
TCCCGCGCGACGACCCTGCACGCCCGCACCATGGAGATCCTCGCCGCGCGCGGCCTGCTC
GAGGCGCTCGGCACCCCGCCGAACGACGTGATGGGCCACTTCGGCGGCGTCCCGCTGGAC
CTCACCCTGCCCACGCCGTACCCCGGCCAGTGGAAGGTCCCGCAGACCCGCACCGAGGAA
CTGCTCCAGGCCTGGGCGCTCTCCCTCGGCGCCACCGTCCGCCGCGGCCACGAACTGCGC
GCGCTGACCGTCACGGACACCGGTGCCGAGGCCGAGGCCACCGGCCCCGACGGCCGGCCC
GTCCGGGTGAGCGCCCGCTACGTCGTCGGCTGCGACGGCGAGCGCAGCACCGTGCGCGAG
CTGACCGGGGCCGACTTCCCCGGGCAGGACGCCACCCGCGAGCTGATCCGCGCCGACGTC
GCCGGCATCGACATCCCCGACCGGCGCTTCCAGCGGCTCCAGCGGGGCCTGGCCATCGCC
GCCCGCCGGCCCGACGGCGTCACCCGGGTGATGGTGCACGAGTTCGGCCGCGCGGCCCGG
CCGCGCACCGGCGCCCCCGCCTTCGCCGAGGTCGTCGACGTGTGGAAGCGCGTGACCGGC
GAGGACATCGGCGGCGGCACCCCGCTGTGGCTCAACGCCTTCGGTGACGCCTCCCGGCAG
GTGGCGCGCTACCGCGACGGCCGCGTGCTGTTCGCCGGGGACGCCGCGCACGTCCAGATG
CCCGTGGGCGGACAGGCCCTCAACCTCGGTCTCCAGGACGCGGTCAACCTCGGCTGGAAG
CTCGCCGCCGAGATCCGGGGCCGGGCCCCGGACGGCCTGCTGGACACGTACCACTCCGAG
CGGCACGCCGTCGGCGAGCGGGTGCTGAGCACCATCCGCGCCCAGTCGACGTTCCTGCTC
GGCGGCCCGGACGTCGAGGCGCTGCGCGAGGTCTTCCGCGAGTTGATCGACCCCGCGCAC
ACCCGTCACACCCGCGCCCACCTGGCCGGCCTGATCAGCGGCCTGGACATCCGGTACGAC
GTCGGCCCGGGCGACCATCCGCTGCTGGGCGCCCGTATGCCCTACGGCGAGCTGGACCAG
GCCCCCGACGCGGCCTGCCGCAAGGCGCGCGGGGTGCTGCTGGACCTCGCGCCCGGCAGC
CCGTCCGCGGCGGAGCTGCACGCCGTCGCCGCCGGCTGGGCGGACCGGGTGGACGTCGTC
ACGGCCGGGTTCCGTACCGCCGACGGACCTTCCGCTCTCTCGGGGGCGCGTGCCGTCCTG
GTGCGGCCCGACGGCCACGTGGTCTGGACCGATTCCGGCGCGGGACGGCCGGAGACGGCC
CTGCGCCGCTGGTTCGGCGCACCGGTGTCTTGA

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09
show BLAST table
InterPro
Database:interpro:38.0
IPR002938 Monooxygenase, FAD-binding (Domain)
 [2-329]  3.90000000000001e-78 PF01494
PF01494   FAD_binding_3
IPR003042 Aromatic-ring hydroxylase-like (Domain)
 [4-26]  6.99997659850661e-42 PR00420 [144-159]  6.99997659850661e-42 PR00420 [266-281]  6.99997659850661e-42 PR00420 [281-297]  6.99997659850661e-42 PR00420 [299-317]  6.99997659850661e-42 PR00420 [317-333]  6.99997659850661e-42 PR00420
PR00420   RNGMNOXGNASE
SignalP
 [1-18]  0.571 Signal
Eukaryota   
TMHMM No significant hit