Rifam_00430 : CDS information

close this sectionLocation

Organism
StrainS699
Entry nameRifamycin
Contig
Start / Stop / Direction85,411 / 86,556 / + [in whole cluster]
85,411 / 86,556 / + [in contig]
Location85411..86556 [in whole cluster]
85411..86556 [in contig]
TypeCDS
Length1,146 bp (381 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category5.1 general function
Productputative glycosyltransferase
Product (GenBank)putative dNTP-hexose glycosyltransferase
Gene
Gene (GenBank)
EC number
Keyword
Note
Note (GenBank)
  • ORF7
Reference
ACC
PmId
[9512878] Biosynthesis of the ansamycin antibiotic rifamycin: deductions from the molecular analysis of the rif biosynthetic gene cluster of Amycolatopsis mediterranei S699. (Chem Biol. , 1998)
comment
ansamycin系抗生物質rifamycinの生合成gene clusterの報告。
Orf7(381aa): dNTP-hexose glycosyl transferase

orf6-10はamino-deoxyhexose nucleotide形成をコードするgenesのようで、Orf7はglycosylatoinを触媒することが想定される。

しかしこれまでにA. mediterranei S699ではglycosylateされたrifamycinは報告されていないのでsilent geneかもしれない。これに一致して、orf6, orf9の不活化はrifamycin B産生に影響しない。

Streptomyces tolypophorusではglycosylated rifamycin derivativesであるtolypomycinsが分離されており、この菌はrifamycin Bも産生する。tolypomycinsのC4に付加する糖4-amino-2,3-dideoxy-L-rhamnoseの生合成後期段階には、 orf6-10によってコードされるような酵素を必要とする。
Related Reference
ACC
Q9ZGC0
NITE
Lando_00200
PmId
[15977274] LanGT2 Catalyzes the First Glycosylation Step during landomycin A biosynthesis. (Chembiochem. , 2005)
[21513888] Rational design of an aryl-C-glycoside catalyst from a natural product O-glycosyltransferase. (Chem Biol. , 2011)
comment
6th, id45%, 5e-74
Streptomyces cyanogenus_lanGT2
Glycosyl transferase homolog
[Lando_00200]D-olivose glycosyltransferase

---
[PMID: 15977274](2005) abstract
lanGT2不活化mutantの産物は糖側鎖を欠損。
よってLanGT2がhexasaccharide生合成においてpriming glycosyl transfer(polyketide骨格のO-8へのD-olivoseの付着)を触媒することを示す。

lanGT2 mutantでurdGT2を発現すると新規C-glycosylated angucyclineが産生されるのを確認している。
よってLanGT2とUrdGT2は似ているが異なる機能を持つ。

---
[PMID: 21513888](2011)
O-glycosyltransferase LanGT2を操作して、UrdGT2のようなC-Glycosylation活性を持つようにしている。
LanGT2, UrdGT2の反応メカニズムを提唱。
ACC
Q9RPA7
NITE
Urd_00200
PmId
[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)
[12696864] The C-Glycosyltransferase UrdGT2 is unselective toward d- and l-configured nucleotide-bound rhodinoses. (J Am Chem Soc. , 2003)
[17640665] Structure and action of the C-C bond-forming glycosyltransferase UrdGT2 involved in the biosynthesis of the antibiotic urdamycin. (J Mol Biol. , 2007)
comment
7th, id44%, 1e-73
Streptomyces fradiae_urdGT2
Glycosyl transferase
[Urd_00200]D-olivose C-glycosyltransferase

[PMID: 10658661](2000)
urdGT2が削除されたmutantは、urdamycin Aの代わりに、C-C connected deoxysugar moietyを欠いたtetracyclic angucyclinonesであるurdamycin I, urdamycin J and urdamycin Kを産生した。したがって、UrdGT2はNDP-D-olivoseのC-glycosyltransferを触媒する。

構造解析など続報あり。

close this sectionSequence

selected fasta
>putative glycosyltransferase [putative dNTP-hexose glycosyltransferase]
MKVLNLAGVAPSTVFSHVPLANALRNAGHQVMTTASVDEMVDTIAGVGLSAVRTTAPGVT
PRQVIAESGLTHVPEDPAEREVMAGRWYAHMEYVTLDALLAFSKDWRPDVIVSGVTSYSG
PLLAAHLGVPYVRHAWDIHTPRLMDQGAEDQLREQLTELGLDGLPEPAMTIEIAPPSLLP
DDLKGGQPMRWIPGNSQSVLEPWMYTKSAGTRIGVTIGTGVANYNQYDFLQAVVEQVATL
DAEVVVAVTEDAAPELRERLKNVRAGWIPLDVVAPTCDVLVHQTGGSTMMTGLSFGVPQV
LLPDPNLFRANAMARRLADTGAAVVLSPEEATSEVIAKTCGELVADPAFKAAAGGLAREI
AELPSPNEVALRIEQLVREAS
selected fasta
>putative glycosyltransferase [putative dNTP-hexose glycosyltransferase]
GTGAAGGTTCTAAATCTCGCCGGGGTCGCCCCGTCGACGGTGTTCAGCCACGTCCCGCTC
GCGAACGCCCTGCGCAACGCCGGGCACCAGGTGATGACCACGGCGTCGGTCGACGAGATG
GTCGACACGATCGCCGGCGTCGGGCTGTCCGCGGTGCGGACCACGGCGCCGGGCGTCACC
CCGCGGCAGGTCATCGCCGAAAGCGGCCTGACGCACGTGCCGGAAGACCCGGCAGAGCGC
GAAGTCATGGCCGGCCGCTGGTACGCGCACATGGAGTACGTGACCCTGGACGCCTTGCTG
GCGTTCAGCAAGGACTGGCGCCCGGACGTCATCGTCAGCGGCGTCACCTCCTACTCCGGC
CCGCTGCTGGCCGCCCACCTCGGCGTGCCGTACGTGCGCCACGCCTGGGACATCCACACC
CCGCGGCTGATGGATCAGGGTGCCGAGGACCAGCTGCGCGAGCAGCTGACGGAACTCGGC
CTGGACGGCCTGCCCGAGCCCGCCATGACGATCGAGATCGCGCCGCCGAGCCTGCTGCCG
GACGACCTCAAGGGCGGCCAGCCGATGCGGTGGATCCCCGGCAACTCGCAGTCGGTGCTG
GAACCGTGGATGTACACCAAGAGCGCGGGCACCCGGATCGGCGTCACCATCGGCACCGGG
GTCGCGAACTACAACCAGTACGACTTCCTGCAGGCCGTCGTCGAACAGGTCGCCACCCTG
GACGCCGAAGTCGTCGTGGCCGTCACCGAAGACGCGGCGCCGGAACTGCGTGAGCGGCTG
AAGAACGTGCGGGCGGGCTGGATCCCGCTGGACGTCGTCGCGCCGACCTGTGACGTCCTG
GTGCACCAGACCGGCGGCAGCACGATGATGACGGGCCTGAGCTTCGGCGTGCCGCAGGTG
CTGCTCCCGGACCCCAACCTCTTCCGCGCCAACGCGATGGCCCGCCGGCTCGCCGACACC
GGCGCCGCGGTCGTGCTCTCGCCCGAGGAAGCCACGAGCGAGGTCATCGCGAAGACGTGC
GGCGAGCTGGTCGCCGACCCGGCGTTCAAGGCGGCCGCGGGCGGGCTCGCCCGGGAGATC
GCCGAGCTGCCCTCGCCGAACGAAGTGGCGCTGCGCATCGAGCAGCTCGTCCGGGAAGCG
TCCTAA

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09
show BLAST table
InterPro
Database:interpro:38.0
IPR004276 Glycosyl transferase, family 28 (Domain)
 [14-136]  4e-06 PF03033
PF03033   Glyco_transf_28
IPR010610 Domain of unknown function DUF1205 (Domain)
 [171-264]  2.2e-21 PF06722
PF06722   DUF1205
SignalP
 [1-21]  0.928 Signal
Bacteria, Gram-negative   
 [1-23]  0.828 Signal
Eukaryota   
 [1-23]  0.429 Signal
Bacteria, Gram-positive   
TMHMM No significant hit
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