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CDS information : Gilvo_00230


close this sectionLocation

Organism
StrainGö 3592
Entry nameGilvocarcin
Contig
Start / Stop / Direction26,199 / 27,554 / + [in whole cluster]
26,199 / 27,554 / + [in contig]
Location26199..27554 [in whole cluster]
26199..27554 [in contig]
TypeCDS
Length1,356 bp (451 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category3.4 other modification
Productputative 2,3-dehydratase
Product (GenBank)putative FAD-dependent oxygenase
Gene
Gene (GenBank)gilOIV
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)
  • GilOIV
Reference
ACC
PmId
[12822997] The complete gene cluster of the antitumor agent gilvocarcin V and its implication for the biosynthesis of the gilvocarcins. (J Am Chem Soc. , 2003)
[15453748] Oxidative rearrangement processes in the biosynthesis of gilvocarcin V. (J Am Chem Soc. , 2004)
[17346045] Multi-oxygenase complexes of the gilvocarcin and jadomycin biosyntheses. (J Am Chem Soc. , 2007)
Related Reference
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
>putative 2,3-dehydratase [putative FAD-dependent oxygenase]
MTEPETSDVLVVGAGPSGLLLAGILAGAGARVTVLEARDAPSPQTRASTLHARAREILDH
HGVEFSPELPWSAHGHYGGLRVDLSRVDSGRAGVWKCPQPELVRTLTGWARGHGARLLHG
EHVESVREQGGRCLVRTRAGTTFSGTLLVAADGRRSTVRSLLGIGCGGAPATRVLVQADV
HGDGLAGRRFERHGRYTVTAAPISPGITRVMLHDPRWPAGEERTLEDLRRAWKESTGETL
PAEPSWSRTFSDDTTVAHPLVKGRVVLCGDAAHPFVPIGGQALNTSLMDAEALGWRVLGY
LDDGDRQGLLDYQDERFSWLTVLAGRLRAQARLLFDTDAAATERKALVAARLAGDADYRR
RIADALAGVDVCYLTPGGAVRRRLSPARLRETGVNPGARRVQRALVPDDGTRTDAWIRPD
HHWYPVARDGARQDWDDAVRLHDDLEPEVTR
selected fasta
>putative 2,3-dehydratase [putative FAD-dependent oxygenase]
ATGACGGAGCCCGAGACCTCGGACGTTCTCGTCGTCGGCGCCGGGCCCAGCGGACTGCTC
CTGGCCGGGATCCTCGCCGGGGCGGGTGCGCGGGTCACGGTGCTGGAGGCGCGGGACGCG
CCCAGCCCGCAGACCCGCGCCTCCACCTTGCACGCCCGTGCCAGGGAGATCCTCGACCAC
CACGGAGTGGAGTTCTCCCCGGAGCTGCCCTGGAGTGCCCACGGACACTACGGCGGCCTG
CGCGTGGACCTCTCCCGGGTCGACTCCGGGCGGGCCGGTGTCTGGAAGTGCCCCCAGCCG
GAACTGGTACGGACGCTGACCGGCTGGGCCCGCGGGCACGGCGCGCGGCTGCTCCACGGG
GAGCACGTGGAGTCCGTCCGCGAGCAGGGCGGGCGCTGTCTGGTGCGTACCCGGGCCGGC
ACCACGTTCAGCGGGACCCTGCTGGTCGCGGCGGACGGCCGGCGGAGCACGGTGCGGTCG
CTGCTGGGCATCGGGTGCGGGGGTGCGCCGGCCACGCGCGTACTGGTGCAGGCCGATGTC
CACGGCGACGGGCTGGCGGGGCGGCGCTTCGAGCGACACGGGCGGTACACCGTGACCGCC
GCACCGATCAGCCCCGGGATCACCCGGGTGATGCTGCACGATCCGCGCTGGCCCGCGGGC
GAGGAACGCACGCTGGAGGACCTCCGTAGAGCCTGGAAGGAGTCCACCGGCGAGACCCTG
CCGGCCGAGCCGTCGTGGTCACGGACCTTCAGCGACGACACGACAGTGGCACACCCGCTG
GTCAAGGGCCGTGTCGTGCTGTGCGGCGACGCCGCCCACCCCTTCGTCCCCATCGGCGGC
CAGGCGCTGAACACGTCGTTGATGGACGCCGAGGCGCTGGGCTGGCGGGTCCTGGGGTAT
CTGGACGACGGGGACCGGCAAGGCCTCCTCGACTACCAGGACGAGCGGTTCTCGTGGCTG
ACCGTTCTCGCGGGGAGACTGCGCGCCCAGGCACGTCTGCTGTTCGACACCGACGCGGCG
GCCACGGAACGCAAGGCGCTGGTCGCCGCGAGACTGGCCGGGGACGCGGACTACCGGCGC
AGGATCGCCGACGCCCTGGCCGGTGTCGACGTGTGCTACCTGACGCCCGGCGGCGCGGTC
CGCCGGCGTCTGTCCCCGGCCCGGCTCCGGGAGACCGGAGTGAACCCCGGCGCCCGCCGC
GTGCAGCGGGCGCTCGTCCCCGACGACGGAACGCGCACGGACGCCTGGATCCGTCCCGAT
CACCACTGGTACCCGGTGGCCCGCGACGGGGCCCGGCAGGACTGGGACGACGCGGTGCGC
CTCCACGACGACTTGGAACCCGAGGTGACGCGGTGA

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09
show BLAST table
InterPro
Database:interpro:38.0
IPR002938 Monooxygenase, FAD-binding (Domain)
 [7-316]  2.29999999999998e-43 PF01494
PF01494   FAD_binding_3
IPR003042 Aromatic-ring hydroxylase-like (Domain)
 [8-30]  9.90001804798395e-25 PR00420 [144-159]  9.90001804798395e-25 PR00420 [262-277]  9.90001804798395e-25 PR00420 [277-293]  9.90001804798395e-25 PR00420 [295-313]  9.90001804798395e-25 PR00420
PR00420   RNGMNOXGNASE
SignalP
 [1-30]  0.608 Signal
Eukaryota   
 [1-30]  0.39 Signal
Bacteria, Gram-positive   
TMHMM No significant hit