Rifam_00360 : CDS information

close this sectionLocation

Organism
StrainS699
Entry nameRifamycin
Contig
Start / Stop / Direction77,187 / 78,119 / + [in whole cluster]
77,187 / 78,119 / + [in contig]
Location77187..78119 [in whole cluster]
77187..78119 [in contig]
TypeCDS
Length933 bp (310 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category5.1 general function
Productputative esterase
Product (GenBank)putative esterase
Gene
Gene (GenBank)
EC number
Keyword
Note
Note (GenBank)
  • ORF2
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。
Orf2(310aa): esterase

Orf2はMycobacteriumの機能不明な遺伝子産物にとても相同性がある。これらはesteraseや、部分的にlipaseに高idである。
Related Reference
ACC
O06441
PmId
[9143135] Molecular analysis of the Rhodococcus sp. strain H1 her gene and characterization of its product, a heroin esterase, expressed in Escherichia coli. (Appl Environ Microbiol. , 1997)
comment
9th, id50%, 1e-68
Rhodococcus sp._her
Heroin esterase

Rhodococcus sp. strain H1のheroin esteraseに関する文献。精製したheroin esteraseのN末端アミノ酸配列よりプライマーを設計してPCRで増幅させてプローブを作成し、サザンブロットによって遺伝子herをクローニングしている。また、得られたher遺伝子をE. coliで発現させて精製し、活性や諸性質を確認している。

close this sectionSequence

selected fasta
>putative esterase [putative esterase]
MVYAFDPELATAVPALPVTDLGDLALARAGVRELRERLPRPDTAGLRIDDVRVPGDGHEV
ALRVYRPVRPRTPAALYFVHGGGFVVGDLDVALVPCVELVRALGIAVVSVDYRLAPETRY
PGPLEDVYTGLCWLVGHAEELGVDPRRIVTYGISSGGCLSGGLALLARDRGGPPIAYQFL
NAPVLDDRLETPSMREFVDTPLWNRPQAEISWDAYLGPGVRATDAVPYYAAPARATDLSG
LPPAYVAVKQFDPLRDEGIAYAVAMQAAGVNVELHLFPGTFHGSARCTDAAISRREQEEQ
FAVLRHVTGR
selected fasta
>putative esterase [putative esterase]
ATGGTCTATGCGTTCGACCCCGAGCTCGCCACCGCAGTGCCGGCCCTGCCGGTCACCGAC
CTCGGCGACCTCGCCCTGGCCCGGGCGGGCGTCCGCGAGCTCAGAGAGCGCTTGCCGAGG
CCGGACACGGCGGGCCTGCGGATCGACGACGTCCGGGTCCCCGGCGACGGGCACGAGGTG
GCGCTGCGCGTCTACCGCCCGGTCCGGCCACGGACGCCGGCGGCCCTGTACTTCGTCCAC
GGCGGCGGGTTCGTGGTCGGCGACCTCGACGTCGCCCTGGTGCCCTGCGTCGAGCTGGTC
CGGGCGCTGGGGATCGCGGTGGTGTCGGTGGACTACCGGCTGGCACCGGAGACGCGCTAC
CCCGGCCCGCTCGAGGACGTCTACACCGGCTTGTGCTGGCTCGTCGGGCACGCGGAGGAG
CTGGGCGTGGACCCGAGGCGGATCGTCACGTACGGCATCAGCTCGGGAGGCTGCCTCAGC
GGCGGCTTGGCCTTGCTGGCCCGCGACCGCGGCGGGCCGCCCATCGCCTACCAGTTCCTG
AACGCCCCGGTCCTGGACGACCGGCTCGAGACGCCGAGCATGCGCGAGTTCGTCGACACG
CCGTTGTGGAACCGGCCGCAGGCCGAGATCAGCTGGGACGCCTACCTCGGACCGGGTGTC
CGGGCTACGGACGCGGTGCCGTACTACGCAGCCCCGGCCCGCGCGACCGACTTGAGCGGG
CTGCCGCCGGCATACGTCGCGGTGAAGCAGTTCGACCCGCTGCGGGACGAAGGGATCGCG
TACGCGGTGGCGATGCAGGCGGCGGGGGTGAACGTCGAGCTGCATCTGTTCCCGGGCACG
TTTCATGGCTCGGCCCGGTGCACGGACGCGGCGATCAGCCGGCGTGAGCAGGAGGAGCAG
TTCGCGGTCCTGCGGCACGTGACCGGCCGCTGA

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09
show BLAST table
InterPro
Database:interpro:38.0
IPR013094 Alpha/beta hydrolase fold-3 (Domain)
 [77-285]  6.1e-62 PF07859
PF07859   Abhydrolase_3
SignalP No significant hit
TMHMM No significant hit
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