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first first   Lando_00020 Lando_00020

CDS information : Lando_00010


close this sectionLocation

Organism
StrainS136
Entry nameLandomycin
Contig
Start / Stop / Direction662 / 2,137 / + [in whole cluster]
662 / 2,137 / + [in contig]
Location662..2137 [in whole cluster]
662..2137 [in contig]
TypeCDS
Length1,476 bp (491 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category3.4 other modification
ProductC-12 hydroxylase/4a,12b-dehydratase
Product (GenBank)oxygenase homolog
Gene
Gene (GenBank)lanE
EC number
Keyword
Note
  • bifunctional protein
Note (GenBank)
  • LanE
Reference
ACC
PmId
[9933932] Cloning and characterization of a gene cluster from Streptomyces cyanogenus S136 probably involved in landomycin biosynthesis. (FEMS Microbiol Lett. , 1999)
[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)
Related Reference
ACC
Q93LY7
PmId
[17654627] Artificial reconstruction of two cryptic angucycline antibiotic biosynthetic pathways. (Chembiochem. , 2007)
[18291320] Sequential action of two flavoenzymes, PgaE and PgaM, in angucycline biosynthesis: chemoenzymatic synthesis of gaudimycin C. (Chem Biol. , 2008)
[21595438] Flavoprotein hydroxylase PgaE catalyzes two consecutive oxygen-dependent tailoring reactions in angucycline biosynthesis. (Biochemistry. , 2011)
ACC
Q54171
NITE
Urd_00100
PmId
[7592377] Cloning and characterization of a polyketide synthase gene from Streptomyces fradiae Tu2717, which carries the genes for biosynthesis of the angucycline antibiotic urdamycin A and a gene probably involved in its oxygenation. (J Bacteriol. , 1995)
[10658661] Two new tailoring enzymes, a glycosyltransferase and an oxygenase, involved in biosynthesis of the angucycline antibiotic urdamycin A in Streptomyces fradiae Tu2717. (Microbiology. , 2000)
[22633416] Tailoring enzymes involved in the biosynthesis of angucyclines contain latent context-dependent catalytic activities. (Chem Biol. , 2012)

close this sectionSequence

selected fasta
>C-12 hydroxylase/4a,12b-dehydratase [oxygenase homolog]
MDAAVIIAGAGPAGLMLAGELRLAGVDVIVLERLARTGESRGLGFTARTMEVFDQRGLLA
RFGDVETSAAGHFGGIPLDFGLLEGAWKAAKTVPQSVTETSLEEWAAELGADIRRGHELL
SLREHGDAVEVEVRGPEGLRTLRAAYLVGCDGGRSTVRKAAGFDFPGTAATLEMFLADVK
GLDLEPRMIGEEAAGGMVMVAKLPGGITRIIAGEYGTSPRRRATPPAYEEIAAVWKRLTG
GDITHGEPVWLSAFGDAARQASEYRRGRVLLAGDSAHIHLPAGGQGMNTSIQDSVNLGWK
LAAVVNGLAGPGLLDSYHSERHPVGERLLMNTRAQGRLLLGGPEVQPLREVLDELVAFEE
VDRHLAGMVSGLEITYDVGAGTPLLGKRMPHLELVGEHAKSSSTELLHHGRCVLLDLADN
ARLREAPRLVGGVDVVTAEPHGVSEDSVLHGTSAVLIRPDGHVAWAAPGSCHDLPMALTR
WFGTPRVGRAF
selected fasta
>C-12 hydroxylase/4a,12b-dehydratase [oxygenase homolog]
ATGGACGCTGCGGTGATCATCGCGGGTGCCGGTCCCGCCGGACTCATGCTCGCCGGTGAG
CTCCGGCTCGCGGGGGTCGACGTCATCGTGCTGGAGCGCCTCGCGAGGACCGGCGAATCC
CGCGGTCTCGGATTCACCGCCCGCACCATGGAGGTGTTCGACCAGCGGGGCCTGCTGGCG
CGCTTCGGTGACGTCGAGACCAGCGCGGCTGGGCACTTCGGGGGAATCCCCCTGGACTTC
GGGCTGCTCGAAGGCGCCTGGAAGGCCGCCAAGACCGTGCCGCAGAGTGTGACGGAGACC
AGTCTGGAGGAGTGGGCGGCCGAGCTGGGTGCGGACATCCGGCGCGGCCACGAACTGCTC
TCCCTGAGGGAGCATGGCGACGCGGTCGAGGTCGAGGTCCGCGGTCCCGAAGGCCTCCGG
ACCCTGCGCGCCGCCTACCTCGTGGGCTGCGACGGCGGCCGCAGCACGGTCCGCAAGGCC
GCGGGATTCGACTTCCCCGGCACCGCGGCCACACTGGAGATGTTCCTCGCCGACGTGAAG
GGGCTCGACCTGGAGCCGCGCATGATCGGCGAGGAAGCTGCCGGCGGCATGGTGATGGTC
GCCAAGCTGCCCGGGGGCATCACCCGCATCATCGCGGGGGAGTACGGGACCTCGCCACGG
CGGCGTGCGACACCGCCGGCTTACGAGGAGATCGCGGCCGTCTGGAAGCGACTGACCGGC
GGCGACATCACGCACGGCGAACCGGTGTGGCTCAGCGCCTTCGGCGACGCCGCGCGTCAG
GCGTCCGAATACCGCCGGGGTCGCGTGTTGCTGGCCGGGGACTCCGCGCACATCCATCTG
CCGGCCGGCGGCCAGGGGATGAACACCAGCATCCAGGACTCGGTGAACCTCGGCTGGAAG
CTGGCCGCCGTCGTCAACGGCTTGGCGGGACCCGGCCTGCTGGACAGCTACCACAGTGAA
CGGCACCCGGTCGGCGAGCGGCTCCTGATGAACACCCGTGCGCAGGGGCGGCTCCTGCTC
GGGGGCCCGGAGGTGCAGCCGCTGCGCGAGGTGCTCGACGAGCTGGTAGCCTTCGAGGAG
GTCGACCGCCACCTCGCCGGCATGGTCAGCGGCCTGGAGATCACGTACGACGTGGGTGCC
GGAACACCGCTGCTCGGCAAGCGCATGCCGCACCTCGAACTGGTCGGCGAGCACGCCAAG
TCCAGCAGTACGGAGCTGCTGCACCACGGCCGGTGCGTGCTCCTCGACCTGGCGGACAAC
GCAAGGCTGCGGGAGGCGCCGCGCCTGGTCGGCGGCGTGGACGTCGTCACGGCAGAGCCG
CACGGGGTGTCCGAGGACAGCGTGCTGCACGGCACGTCCGCCGTGCTGATCCGGCCCGAC
GGCCACGTCGCCTGGGCGGCCCCGGGCAGTTGTCACGACCTGCCCATGGCCCTGACGCGC
TGGTTCGGTACACCGCGGGTCGGGCGCGCCTTCTGA

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09
show BLAST table
InterPro
Database:interpro:38.0
IPR002938 Monooxygenase, FAD-binding (Domain)
 [3-331]  5.99999999999995e-86 PF01494
PF01494   FAD_binding_3
IPR003042 Aromatic-ring hydroxylase-like (Domain)
 [4-26]  1.10000150671643e-45 PR00420 [143-158]  1.10000150671643e-45 PR00420 [266-281]  1.10000150671643e-45 PR00420 [281-297]  1.10000150671643e-45 PR00420 [299-317]  1.10000150671643e-45 PR00420 [317-333]  1.10000150671643e-45 PR00420
PR00420   RNGMNOXGNASE
SignalP No significant hit
TMHMM No significant hit
first first   Lando_00020 Lando_00020