close all open/close all

CDS information : Lasal_00210


close this sectionLocation

Organism
StrainATCC 35851
Entry nameLasalocid
Contig
Start / Stop / Direction77,627 / 78,475 / + [in whole cluster]
77,627 / 78,475 / + [in contig]
Location77627..78475 [in whole cluster]
77627..78475 [in contig]
TypeCDS
Length849 bp (282 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category3.4 other modification
Productepoxide hydrolase/cyclase
Product (GenBank)epoxide hydrolase
Gene
Gene (GenBank)lsd19
EC number
Keyword
Note
  • N-terminal domain belongs to polyether epoxide hydrolase(PEH)-A group.
  • C-terminal domain belongs to polyether epoxide hydrolase(PEH)-B group.
Note (GenBank)
Reference
ACC
PmId
[19129623] Identification of a gene cluster of polyether antibiotic lasalocid from Streptomyces lasaliensis. (Biosci Biotechnol Biochem. , 2009)
[18710235] Epoxide hydrolase Lsd19 for polyether formation in the biosynthesis of lasalocid A: direct experimental evidence on polyene-polyepoxide hypothesis in polyether biosynthesis. (J Am Chem Soc. , 2008)
[20394359] Intriguing substrate tolerance of epoxide hydrolase Lsd19 involved in biosynthesis of the ionophore antibiotic lasalocid A. (Org Lett. , 2010)
[21375229] Enzymatic epoxide-opening cascades catalyzed by a pair of epoxide hydrolases in the ionophore polyether biosynthesis. (Org Lett. , 2011)
[22388816] Enzymatic catalysis of anti-Baldwin ring closure in polyether biosynthesis. (Nature. , 2012)
[23796908] Biosynthetic machinery of ionophore polyether lasalocid: enzymatic construction of polyether skeleton. (Curr Opin Chem Biol. , 2013)
[25535803] Epoxide hydrolase-lasalocid a structure provides mechanistic insight into polyether natural product biosynthesis. (J Am Chem Soc. , 2015)
Related Reference
ACC
B5M9L7
NITE
Lasal2_00250
PmId
[19025863] Analysis of specific mutants in the lasalocid gene cluster: evidence for enzymatic catalysis of a disfavoured polyether ring closure. (Chembiochem. , 2008)
[22025396] Insights into lasalocid A ring formation by chemical chain termination in vivo. (Angew Chem Int Ed Engl. , 2011)

close this sectionSequence

selected fasta
>epoxide hydrolase/cyclase [epoxide hydrolase]
MPAETVRKEVALEYCRRVNAGELEGVLQLFAPDALLVDPLGTEPVVGRAALAARLAPALR
GAVHEEPGRPYAAHDGTSVVLPATVTVGAPGAPPQRRGRTRVMGVIEVGEDGLIREMRVM
WGVTDSSWTARPAPDEERRKELAREHCLRINDGDVDGLLKLYSPRIRFEDPVGSWTRTGL
EALRAHATMAVGSNVRETAGLTVAGQDGRHAAVTVSATMDYLPSGPLLARHHLMTLPAPA
DPHRALIGIEYVMVIGVDADGLIDEMRAYWGATDVSLLDPAA
selected fasta
>epoxide hydrolase/cyclase [epoxide hydrolase]
ATGCCTGCGGAGACGGTGCGCAAGGAAGTGGCCCTGGAGTACTGCCGCAGGGTCAACGCC
GGTGAACTGGAGGGCGTGCTCCAGCTGTTCGCGCCGGACGCCCTGCTGGTGGACCCGCTG
GGCACCGAGCCGGTCGTCGGCCGCGCCGCCCTCGCCGCCCGGCTGGCCCCGGCGTTGCGC
GGAGCCGTGCACGAGGAGCCGGGGCGCCCGTACGCGGCTCATGACGGCACCTCCGTCGTG
CTGCCGGCGACCGTCACGGTCGGCGCCCCGGGCGCTCCGCCGCAGCGGCGGGGACGGACC
CGGGTGATGGGCGTCATCGAGGTGGGCGAGGACGGCCTGATCCGGGAGATGCGCGTCATG
TGGGGGGTCACGGACTCGTCGTGGACCGCCCGTCCCGCCCCCGACGAGGAACGCCGCAAG
GAGCTGGCCCGCGAGCACTGCCTGCGCATCAACGACGGTGACGTGGACGGTCTGCTCAAG
CTGTACTCGCCCCGCATCCGCTTCGAGGACCCCGTCGGCTCCTGGACCCGCACCGGCCTG
GAGGCGCTGCGGGCCCACGCGACGATGGCGGTGGGCAGCAACGTGCGGGAGACGGCCGGG
CTGACGGTCGCCGGTCAGGACGGACGGCACGCGGCCGTCACGGTCTCCGCGACGATGGAC
TACCTGCCCTCGGGGCCCCTGTTGGCCCGCCACCACCTCATGACGCTCCCGGCCCCCGCC
GATCCGCACCGGGCCCTCATCGGCATCGAGTACGTGATGGTGATCGGCGTCGATGCCGAC
GGCCTCATCGACGAGATGCGCGCCTACTGGGGGGCAACGGACGTCTCCCTGCTCGATCCT
GCCGCCTAG

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09
show BLAST table
InterPro
Database:interpro:38.0
IPR009959 Polyketide cyclase SnoaL-like domain (Domain)
 [13-117]  3.5e-12 PF12680 [149-265]  4.20000000000001e-07 PF12680
PF12680   SnoaL_2
SignalP
 [1-36]  0.059 Signal
Eukaryota   
 [1-36]  0.05 Signal
Bacteria, Gram-negative   
TMHMM No significant hit