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CDS information : Jado_00130


close this sectionLocation

Organism
StrainISP5230 (=NBRC 13096)
Entry nameJadomycin B
Contig
Start / Stop / Direction13,313 / 14,851 / + [in whole cluster]
1 / 1,539 / + [in contig]
Location13313..14851 [in whole cluster]
1..1539 [in contig]
TypeCDS
Length1,539 bp (512 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category3.4 other modification
Product2,3-dehydratase
Product (GenBank)JadF
Gene
Gene (GenBank)jadF
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)
  • bifunctional monooxygenase-dehydratase
Reference
ACC
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 [JadF]
MTEPRRAGAPAPESPDAPDTPVLLDADVVVIGAGPTGLMLAGELRLGGADVIVLESRETP
TTESRASTLHARTMELLDDRGLLTPLGTPPSEPRGHFGGIPLDLTLPGRHPGQWKVEQTR
TEALLQEWATGLGADVRRGHTLRSLTVTETYAEAGATGPGGRDVRVRARYAVGCDGERST
VRALAGAEFPGQEARRELLRADVAGIDVPDRRFQRLPGGLAVAACRNGVTRVMVHEFGRP
AVARTGEPEFAEVVDVWKRVTGEDISGGTPLWVNSFHDANRQLTRYRDGRVLWAGDAAHQ
QMPIGGQALNLGLQDAVNLGWKLAAVVRGTAPDGLLDTYHDERHAVGRQVLGNIRAQALL
LLGGPEAEPVRSLLGPLIALDDVRAHLAGKVSGLDIRYGAGAADVHPLTGTRLPRTALVD
DGREAVDPSLRAGQGLFLTLDPSGTGPGTGAAAAAAWAGRVGTAVARPVPGGVLDGLDAV
LVRPDGYLAWTSADGAGPEAALHRWFGAPTHL
selected fasta
>2,3-dehydratase [JadF]
ATGACGGAGCCCCGCCGGGCAGGAGCGCCCGCACCGGAGTCCCCGGACGCCCCGGACACC
CCGGTCCTCCTGGACGCCGACGTCGTCGTCATCGGCGCCGGGCCCACCGGCCTGATGCTC
GCCGGCGAACTGCGGCTCGGCGGCGCGGACGTGATCGTCCTGGAGAGCCGGGAGACCCCC
ACCACCGAGTCCCGGGCCTCCACGCTGCACGCCCGCACGATGGAACTGCTCGACGACCGC
GGGCTGCTCACCCCGCTCGGCACTCCGCCGTCGGAGCCCCGCGGGCACTTCGGCGGCATC
CCGCTCGACCTGACCCTGCCCGGTCGGCACCCCGGGCAGTGGAAGGTCGAGCAGACCCGG
ACCGAGGCGCTGCTCCAGGAGTGGGCCACCGGCCTCGGGGCCGACGTCCGACGCGGCCAC
ACCCTGCGCTCCCTCACGGTGACGGAGACGTACGCCGAGGCCGGAGCCACCGGCCCCGGC
GGCCGTGACGTGCGCGTGCGGGCCCGGTACGCCGTGGGCTGCGACGGGGAGCGGAGCACC
GTACGGGCCCTGGCCGGGGCGGAGTTCCCCGGCCAGGAGGCCCGGCGCGAACTGCTCCGG
GCCGATGTGGCCGGGATCGACGTCCCCGACCGGCGCTTCCAGCGGCTGCCCGGCGGACTG
GCCGTCGCCGCGTGCCGCAACGGCGTCACCCGGGTCATGGTCCACGAGTTCGGCAGGCCC
GCCGTGGCCAGGACCGGCGAGCCGGAGTTCGCCGAGGTCGTGGACGTGTGGAAGCGGGTC
ACGGGGGAGGACATCAGCGGCGGCACGCCGCTCTGGGTGAACTCCTTCCACGACGCCAAC
CGGCAGCTCACCCGCTACCGGGACGGGCGCGTCCTGTGGGCGGGGGACGCCGCCCACCAG
CAGATGCCGATCGGCGGCCAGGCCCTCAACCTGGGGCTCCAGGACGCCGTCAACCTCGGC
TGGAAGCTCGCCGCCGTGGTCCGCGGCACGGCGCCGGACGGGCTGCTCGACACCTACCAC
GACGAGCGGCACGCCGTCGGCCGCCAGGTCCTCGGCAACATCAGGGCCCAGGCCCTGCTG
CTCCTCGGCGGGCCCGAGGCGGAGCCCGTCCGCTCCCTCCTCGGCCCGCTCATCGCCCTG
GACGACGTGCGGGCGCACCTGGCCGGCAAGGTCTCAGGACTCGACATCCGGTACGGGGCC
GGGGCGGCGGACGTGCATCCGCTGACCGGCACCCGGCTGCCCCGCACGGCCCTCGTGGAC
GACGGCCGCGAGGCCGTCGACCCGTCGCTGCGGGCCGGCCAGGGCCTGTTCCTGACGCTG
GACCCGAGCGGCACCGGGCCCGGGACCGGAGCGGCGGCGGCCGCCGCCTGGGCCGGCCGG
GTCGGCACCGCCGTGGCCAGGCCCGTGCCCGGCGGCGTCCTCGACGGACTCGACGCCGTC
CTCGTACGGCCCGACGGCTACCTCGCCTGGACCTCGGCCGACGGCGCGGGACCGGAAGCG
GCCCTGCACCGCTGGTTCGGCGCCCCCACCCACCTCTGA

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09
show BLAST table
InterPro
Database:interpro:38.0
IPR002938 Monooxygenase, FAD-binding (Domain)
 [26-351]  1.7e-72 PF01494
PF01494   FAD_binding_3
IPR003042 Aromatic-ring hydroxylase-like (Domain)
 [27-49]  2.9e-41 PR00420 [167-182]  2.9e-41 PR00420 [288-303]  2.9e-41 PR00420 [303-319]  2.9e-41 PR00420 [321-339]  2.9e-41 PR00420 [339-355]  2.9e-41 PR00420
PR00420   RNGMNOXGNASE
SignalP No significant hit
TMHMM No significant hit