Rifam_00540 : CDS information

close this sectionLocation

Organism
StrainS699
Entry nameRifamycin
Contig
Start / Stop / Direction96,813 / 96,034 / - [in whole cluster]
96,813 / 96,034 / - [in contig]
Locationcomplement(96034..96813) [in whole cluster]
complement(96034..96813) [in contig]
TypeCDS
Length780 bp (259 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category1.4 Other
Producttype II thioesterase
Product (GenBank)RifR
Gene
Gene (GenBank)rifR
EC number
Keyword
  • type II thioesterase
Note
Note (GenBank)
  • putative thioesterase; similar to the thioesterase of Streptomyces fradiae (strain T59235)
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)
[10908112] Thioesterases and the premature termination of polyketide chain elongation in rifamycin B biosynthesis by Amycolatopsis mediterranei S699. (J Antibiot (Tokyo). , 2000)
[19103602] Structure and functional analysis of RifR, the type II thioesterase from the rifamycin biosynthetic pathway. (J Biol Chem. , 2009)
comment
[PMID: 9512878](1998)
ansamycin系抗生物質rifamycinの生合成gene clusterの報告。
Orf12(252aa): thioesterase

--
[PMID: 10908112](2000)
rifamycin PKSが容易に未熟なpolyketide鎖中間体を放出することについて検討。
RifR thioesterase 2はこれに関与しない。未熟な中間体の放出はRif PKS自身の特性である。

正常なunitで伸長しているけど未熟なまま放出される場合の話。

--
[PMID: 19103602](2009)
orf12=rifR

RifRは、acyl-CoAsよりもacyl carrier domainのphosphopantetheinyl armからのacyl unitsを加水分解する(Steady-state kinetics)。
helical lidの運動が、RifR active siteへの基質のアクセスを調節する(立体構造解析)。

RifRがCoA基質よりACP基質への反応を好むことは、type II thioesteraseがcarrier domainsから異常unitsを除くようなhousekeeping functionsをすると考えられていることに一致する。

close this sectionSequence

selected fasta
>type II thioesterase [RifR]
MHRPEAEKWLRRFERAPDARARLVCLPHAGGSASFFFPLAKALAPAVEVLAVQYPGRQDR
RHEPPVDSIGGLTNRLLEVLRPFGDRPLALFGHSMGAIIGYELALRMPEAGLPAPVHLFA
SGRRAPSRYRDDDVRGASDERLVAELRKLGGSDAAMLADPELLAMVLPAIRSDYRAVETY
RHEPGRRVDCPVTVFTGDHDPRVSVGEARAWEEHTTGPADLRVLPGGHFFLVDQAAPMIA
TMTEKLAGPALTGSTGGNS
selected fasta
>type II thioesterase [RifR]
GTGCACCGACCAGAAGCCGAGAAGTGGTTGCGCCGTTTCGAACGGGCACCGGACGCGCGA
GCCCGGCTCGTGTGCCTGCCCCACGCCGGCGGCTCGGCCAGCTTCTTCTTCCCGCTCGCC
AAGGCCCTCGCTCCCGCGGTGGAGGTCCTGGCGGTCCAGTACCCGGGCCGCCAGGACCGG
CGGCACGAGCCGCCCGTCGACAGCATCGGCGGGCTGACGAACCGGCTGCTGGAGGTGCTG
CGCCCGTTCGGCGACCGGCCGCTGGCGTTGTTCGGGCACAGCATGGGCGCGATCATCGGC
TACGAACTGGCGTTGCGGATGCCCGAAGCCGGGCTGCCCGCGCCGGTGCACCTGTTCGCG
TCCGGGCGGCGGGCGCCCTCGCGCTACCGCGACGACGACGTGCGCGGCGCGTCGGACGAA
CGGCTCGTAGCCGAGCTGCGGAAGCTCGGCGGTTCCGACGCGGCCATGCTCGCCGACCCC
GAACTGCTGGCCATGGTCCTGCCCGCGATCCGCAGCGACTACCGCGCGGTGGAGACCTAC
CGGCACGAGCCCGGACGGCGGGTGGACTGCCCCGTCACGGTGTTCACCGGCGACCACGAT
CCGCGCGTGTCGGTCGGCGAAGCCCGCGCCTGGGAAGAGCACACCACCGGGCCGGCCGAC
CTGCGGGTGCTGCCGGGCGGTCACTTCTTCCTGGTGGACCAGGCCGCCCCGATGATCGCG
ACGATGACGGAGAAGCTGGCCGGCCCCGCGCTGACCGGATCCACGGGAGGGAACTCGTGA

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09
show BLAST table
InterPro
Database:interpro:38.0
IPR001031 Thioesterase (Domain)
 [22-244]  3.29999999999997e-56 PF00975
PF00975   Thioesterase
SignalP No significant hit
TMHMM No significant hit
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