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CDS information : Lando_00310


close this sectionLocation

Organism
StrainS136
Entry nameLandomycin
Contig
Start / Stop / Direction31,955 / 33,148 / + [in whole cluster]
31,955 / 33,148 / + [in contig]
Location31955..33148 [in whole cluster]
31955..33148 [in contig]
TypeCDS
Length1,194 bp (397 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category3.3 modification reduction
Productputative FMNH2-dependent monooxygenase
Product (GenBank)oxygenase homolog
Gene
Gene (GenBank)lanZ5
EC number
Keyword
  • two-component system
  • C-11 hydroxylate
Note
  • This gene product have been identified to have 5,6-dehydration activity, which yields minor landomycin derivatives.
Note (GenBank)
  • LanZ5
Reference
ACC
PmId
[9933932] Cloning and characterization of a gene cluster from Streptomyces cyanogenus S136 probably involved in landomycin biosynthesis. (FEMS Microbiol Lett. , 1999)
[15812784] Generation of novel landomycins M and O through targeted gene disruption. (Chembiochem. , 2005)
[22454092] Elucidation of post-PKS tailoring steps involved in landomycin biosynthesis. (Org Biomol Chem. , 2012)
Related Reference
ACC
Q6T1C5
PmId
[15123249] Generation of new landomycins by combinatorial biosynthetic manipulation of the LndGT4 gene of the landomycin E cluster in S. globisporus. (Chem Biol. , 2004)
ACC
Q53907
NITE
Actino_00110
PmId
[18245777] Mechanism and regulation of the Two-component FMN-dependent monooxygenase ActVA-ActVB from Streptomyces coelicolor. (J Biol Chem. , 2008)
[19246012] Biosynthesis of actinorhodin and related antibiotics: discovery of alternative routes for quinone formation encoded in the act gene cluster. (Chem Biol. , 2009)
[22086671] Epoxyquinone formation catalyzed by a two-component flavin-dependent monooxygenase involved in biosynthesis of the antibiotic actinorhodin. (Chembiochem. , 2011)
[23601640] Biosynthetic conclusions from the functional dissection of oxygenases for biosynthesis of actinorhodin and related streptomyces antibiotics. (Chem Biol. , 2013)

close this sectionSequence

selected fasta
>putative FMNH2-dependent monooxygenase [oxygenase homolog]
MRTNNDVGTVEETVTSPQKAGTLLSAAEDVAALAGDQAARADETRRLDPDVMKVVLGRRF
ARHFVPVEHGGAAGTFTELTEALVTVGTACAASSWSASIVAGVGRMAGFLPAEGRAEVWK
DGPDAVVVGSLAPLGRAKAVPGGWRLSGTWPSISVVDFSDWALVRAVVADSEGQALRVFV
VPRAGYEIQDTWSNVGMRATGSNTLVVDDVFVPDARTFEGDDLFQGRPRSSSAACHSVPL
QAVNGLSFAAPALGAARGALAVWSDYATAKFRSAPREPGGPGISRGFYATTLARAAGEID
MAYLLLDRAGRVADRGAGVTPLEAPRNTRDCALAVETSVTAVNRIFAAAGTSGHSTASSL
QRFWRDANAAATHIGLQFEPAAMAYASAVSAHLPDTK
selected fasta
>putative FMNH2-dependent monooxygenase [oxygenase homolog]
ATGAGAACGAACAACGACGTCGGGACAGTGGAGGAAACAGTGACGTCACCACAGAAGGCA
GGGACCCTGCTCAGCGCGGCCGAGGACGTCGCTGCCCTGGCAGGTGACCAGGCGGCCCGC
GCGGACGAGACGCGCCGCCTCGACCCGGATGTCATGAAGGTCGTGCTCGGGCGCCGCTTC
GCCCGGCACTTCGTCCCCGTGGAACACGGTGGTGCGGCGGGCACGTTCACTGAGCTCACC
GAGGCCCTGGTCACGGTGGGGACGGCCTGTGCCGCCTCGTCCTGGAGCGCCTCGATCGTC
GCGGGCGTCGGCCGGATGGCGGGCTTCCTGCCCGCCGAGGGGCGTGCGGAGGTGTGGAAG
GACGGCCCGGATGCCGTGGTGGTCGGCTCGCTCGCGCCGCTGGGCAGGGCCAAGGCGGTG
CCGGGCGGCTGGCGGCTGTCCGGCACATGGCCCTCCATCAGCGTTGTCGACTTCTCCGAC
TGGGCGCTGGTGCGTGCGGTGGTTGCGGACAGCGAGGGCCAGGCGCTACGCGTCTTCGTG
GTCCCGCGGGCCGGCTACGAGATTCAGGACACCTGGTCCAACGTCGGCATGCGTGCGACC
GGCAGCAACACACTCGTCGTCGACGACGTCTTCGTCCCCGACGCGCGGACCTTCGAAGGA
GACGACCTCTTCCAAGGGCGTCCCCGCAGCTCGTCCGCTGCCTGCCACAGTGTCCCGCTG
CAGGCCGTCAACGGTCTCTCCTTTGCGGCGCCGGCCCTGGGTGCCGCACGCGGGGCACTC
GCCGTCTGGTCGGATTACGCCACGGCGAAGTTCCGCAGTGCACCGAGGGAGCCTGGCGGC
CCGGGAATCAGTCGCGGCTTCTACGCGACCACGCTGGCACGTGCGGCCGGGGAAATCGAT
ATGGCGTACCTGCTGCTCGACAGGGCCGGCAGGGTTGCCGACCGGGGTGCAGGCGTGACA
CCGCTGGAAGCGCCCCGCAACACGCGTGACTGCGCCCTGGCCGTCGAGACCTCGGTGACC
GCGGTGAACCGGATATTCGCTGCCGCTGGTACCAGCGGTCACTCCACCGCAAGCTCGCTT
CAGCGCTTCTGGCGGGATGCCAACGCCGCGGCCACCCATATCGGCCTGCAGTTCGAGCCC
GCCGCGATGGCCTACGCGTCGGCGGTCTCGGCACACCTGCCCGACACGAAGTAG

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09
show BLAST table
InterPro
Database:interpro:38.0
IPR006091 Acyl-CoA oxidase/dehydrogenase, central domain (Domain)
 [129-211]  3.8e-27 G3DSA:2.40.110.10
G3DSA:2.40.110.10   Acyl_CoA_DH/ox_M
IPR009075 Acyl-CoA dehydrogenase/oxidase C-terminal (Domain)
 [212-389]  1.2e-36 G3DSA:1.20.140.10
G3DSA:1.20.140.10   AcylCoA_DH_1/2_C
 [246-375]  8.69999350765688e-11 SSF47203
SSF47203   AcylCoADH_C_like
IPR009100 Acyl-CoA dehydrogenase/oxidase (Domain)
 [12-220]  3.80000697093586e-26 SSF56645
SSF56645   AcylCoA_dehyd_NM
IPR013107 Acyl-CoA dehydrogenase, type 2, C-terminal (Domain)
 [246-377]  4.6e-39 PF08028
PF08028   Acyl-CoA_dh_2
IPR013786 Acyl-CoA dehydrogenase/oxidase, N-terminal (Domain)
 [15-125]  9.8e-23 G3DSA:1.10.540.10
G3DSA:1.10.540.10   AcylCoA_DH/ox_N
SignalP
 [1-34]  0.121 Signal
Bacteria, Gram-negative   
TMHMM No significant hit