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CDS information : Ovied_00090


close this sectionLocation

Organism
StrainATCC 11891
Entry nameOviedomycin
Contig
Start / Stop / Direction7,963 / 9,447 / + [in whole cluster]
7,963 / 9,447 / + [in contig]
Location7963..9447 [in whole cluster]
7963..9447 [in contig]
TypeCDS
Length1,485 bp (494 aa)
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close this sectionAnnotation

Category3.4 other modification
Product4a,12b-dehydratase/C-12 hydroxylase
Product (GenBank)oxygenase
Gene
Gene (GenBank)ovmOI
EC number
Keyword
Note
  • bifunctional protein
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
Q9ZGD9
NITE
Lando_00010
PmId
[22633416] Tailoring enzymes involved in the biosynthesis of angucyclines contain latent context-dependent catalytic activities. (Chem Biol. , 2012)
[22454092] Elucidation of post-PKS tailoring steps involved in landomycin biosynthesis. (Org Biomol Chem. , 2012)
ACC
Q5U913
NITE
Jado_00150
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)
[20422670] Characterization of JadH as an FAD- and NAD(P)H-dependent bifunctional hydroxylase/dehydrase in jadomycin biosynthesis. (Chembiochem. , 2010)
[22633416] Tailoring enzymes involved in the biosynthesis of angucyclines contain latent context-dependent catalytic activities. (Chem Biol. , 2012)

close this sectionSequence

selected fasta
>4a,12b-dehydratase/C-12 hydroxylase [oxygenase]
MDAALVDVPVVIVGAGPTGLMLAGELRLAGVEIVVIDRLPRPSGESRGLGFTPRTMEVFD
QRGLLPRFGEIVTSKLGHFGGTPVDFGVLDGAHFSVKDVPQHRTEAVLGAWLAELGVQVR
RGRELVALTAGEDGVRIDIEGPDGPERLRAGYLVGCDGGRSTVRRLAGFDFPGTAATMEM
YLADITDCEVRPRPIGESVPGGMAMSVPIGDGVHRIIACERDNPPRERTGPPPFAEVAAA
WQRLTHQDTAAPPGVGQRFGNAARQVTEYRRGRVLLAGDAAHIHLPAGGQGMNTGIQDAV
NLGWKLAAVVRGTAPEALLDTYHAERHPVGRRLLTNTQAQGLLYLSGSEMQPLRDVLAEL
IAYEDVSRHLAGMISGLDIRYDVGATDHPLPGRRMPHLELVTADGGKTSTTALLHSARGL
LLDLADDPGTRRAAAGWADRVDTVTATPHDTAQDRPPHGATAVLVRPDGHVAWAAPGGPG
ELTAALERWFGPSR
selected fasta
>4a,12b-dehydratase/C-12 hydroxylase [oxygenase]
ATGGACGCTGCCCTCGTCGACGTTCCCGTGGTCATCGTGGGAGCAGGCCCCACGGGGCTG
ATGCTCGCCGGTGAACTGCGCCTCGCCGGAGTCGAGATCGTCGTCATCGACCGCCTTCCC
CGGCCCAGCGGAGAGTCCCGCGGGCTCGGTTTCACCCCTCGCACCATGGAGGTCTTCGAC
CAGCGCGGACTGCTGCCCCGCTTCGGCGAGATCGTCACCAGCAAGCTCGGCCACTTCGGC
GGCACCCCCGTCGACTTCGGCGTGCTCGACGGCGCCCACTTCAGCGTCAAGGACGTGCCC
CAGCACCGTACGGAGGCGGTGCTCGGCGCATGGCTCGCCGAACTCGGCGTCCAGGTGCGG
CGCGGCCGCGAACTCGTCGCCCTCACGGCCGGCGAGGACGGCGTCCGCATCGACATCGAG
GGCCCCGACGGCCCCGAACGGCTGCGCGCCGGCTACCTGGTGGGCTGCGACGGCGGCCGC
AGCACGGTCCGCAGACTCGCCGGGTTCGACTTCCCCGGCACCGCCGCGACCATGGAGATG
TACCTCGCCGACATCACCGACTGCGAGGTGCGGCCCCGCCCCATCGGCGAGTCCGTGCCC
GGCGGGATGGCCATGTCGGTGCCCATCGGCGACGGCGTCCACCGCATCATCGCGTGCGAG
CGCGACAACCCCCCGCGCGAACGCACCGGACCGCCGCCCTTCGCGGAGGTCGCCGCCGCC
TGGCAGCGCCTGACCCACCAGGACACAGCGGCGCCACCCGGTGTGGGTCAGCGCTTCGGC
AACGCCGCCCGCCAGGTCACCGAGTACCGCCGCGGACGCGTCCTGCTGGCCGGCGACGCG
GCGCACATCCACCTGCCCGCCGGCGGCCAGGGCATGAACACCGGCATCCAGGACGCCGTC
AACCTGGGCTGGAAGCTCGCCGCCGTCGTACGCGGCACGGCCCCCGAGGCGCTGCTCGAC
ACCTACCACGCCGAGCGCCACCCGGTCGGCCGCCGGCTGCTGACCAACACGCAGGCCCAG
GGCCTGCTCTACCTCAGCGGCAGCGAGATGCAGCCGCTGCGCGACGTGCTCGCCGAGCTG
ATCGCGTACGAGGACGTCAGCCGCCACCTCGCCGGAATGATCAGCGGCCTGGACATCCGC
TACGACGTCGGCGCGACCGATCACCCGCTGCCCGGCCGCCGCATGCCGCACCTGGAACTC
GTGACCGCCGACGGCGGCAAGACCAGCACCACCGCCCTGCTGCACAGCGCGCGCGGCTTG
CTGCTCGACCTCGCCGACGACCCCGGGACCCGGCGCGCCGCCGCCGGCTGGGCGGACCGC
GTGGACACCGTCACCGCGACCCCGCACGACACCGCCCAGGACCGGCCGCCGCACGGCGCC
ACCGCCGTACTGGTGCGCCCCGACGGCCATGTGGCCTGGGCCGCGCCCGGCGGTCCCGGG
GAGCTGACCGCCGCCCTGGAGCGCTGGTTCGGCCCGTCCCGCTGA

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09
show BLAST table
InterPro
Database:interpro:38.0
IPR002938 Monooxygenase, FAD-binding (Domain)
 [7-336]  1.10000000000001e-85 PF01494
PF01494   FAD_binding_3
IPR003042 Aromatic-ring hydroxylase-like (Domain)
 [9-31]  1.49999648196323e-48 PR00420 [149-164]  1.49999648196323e-48 PR00420 [271-286]  1.49999648196323e-48 PR00420 [286-302]  1.49999648196323e-48 PR00420 [304-322]  1.49999648196323e-48 PR00420 [322-338]  1.49999648196323e-48 PR00420
PR00420   RNGMNOXGNASE
SignalP No significant hit
TMHMM No significant hit