Gene_Locus Report

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Gene_locus Report for: 9bact-g3cr02

environmental samples uncultured bacterium Esterase estDL136

Comment
Other strains: environmental samples uncultured bacterium (pDL136) EstDL136 reactivated chloramphenicol from its acetyl derivates by counteracting the chloramphenicol acetyltransferase (CAT) activity. It catalyzed the deacetylation of 1- and 3- acetyl and 1,3-diacetyl derivates.EstDL136 also acts as a chloramphenicol hydrolase.It cleaves the amide linkage at C2 of chloramphenicol and thereby confers Cm resistance to bacteria


Relationship
Family|Hormone-sensitive_lipase_like
Block| H
Position in NCBI Life Tree|uncultured bacterium
(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.)
> cellular organisms: N E > Bacteria: N E > environmental samples: N E > uncultured bacterium: N E
Warning: This entry is a compilation of different species or line or strain with more than 90% amino acide identity. You can retrieve all strain data


Molecular evidence
Database
No mutation
2 structures: 6AAE, 6IEY
No kinetic





2 substrates: Chloramphenicol, Florfenicol
No inhibitor
2 Structure : 6AAE, 6IEY
2 UniProt : G3CR02, I6N3G4
2 Interpro : G3CR02, I6N3G4
2 Prodom : G3CR02, I6N3G4
2 Pfam : G3CR02, I6N3G4
2 PIRSF : G3CR02, I6N3G4
2 SUPERFAM : G3CR02, I6N3G4
Sequence
Graphical view for this peptide sequence: 9bact-g3cr02
Colored MSA for Hormone-sensitive_lipase_like (raw)
MPLNPHVEALLQMMAQMPAPDFSVANPAEIRAVFDNPMPLAAPPQVARVE
NIAISLDGRDLDARLYVPEDADERPALMVYYHGGGWVIGTLDTHDGTCRA
LAQKSGCAVLSIAYRLAPEYRYPAPAEDCYDALVWAKQNAATLGVDGDRL
AVGGDSAGGNLAAAVAIMARDRNGPALRHQLLIYPVTDNDFTLASYAENG
GGEYYLSTDGMRWFWGHYLGDTAAENAPLAAVLNVADLSGLAPATVITAE
YDPLRDEGIAYAKKLDAAGVPVDAATAPGMIHGFFSMFEAVPDSWEWIER
GASNLKRDLA
Legend This sequence has been compared to family alignement (MSA)
red => minority aminoacid
blue => majority aminoacid
color intensity => conservation rate
title => sequence position(MSA position)aminoacid rate
Catalytic site
Catalytic site in the MSA

MPLNPHVEALLQMMAQMPAPDFSVANPAEIRAVFDNPMPLAAPPQVARVE
NIAISLDGRDLDARLYVPEDADERPALMVYYHGGGWVIGTLDTHDGTCRA
LAQKSGCAVLSIAYRLAPEYRYPAPAEDCYDALVWAKQNAATLGVDGDRL
AVGGDSAGGNLAAAVAIMARDRNGPALRHQLLIYPVTDNDFTLASYAENG
GGEYYLSTDGMRWFWGHYLGDTAAENAPLAAVLNVADLSGLAPATVITAE
YDPLRDEGIAYAKKLDAAGVPVDAATAPGMIHGFFSMFEAVPDSWEWIER
GASNLKRDLA


References
    Title: Crystal structure of chloramphenicol-metabolizing enzyme EstDL136 from a metagenome
    Kim SH, Kang PA, Han K, Lee SW, Rhee S
    Ref: PLoS ONE, 14:e0210298, 2019 : PubMed

            

    Title: Inactivation of chloramphenicol and florfenicol by a novel chloramphenicol hydrolase
    Tao W, Lee MH, Wu J, Kim NH, Kim JC, Chung E, Hwang EC, Lee SW
    Ref: Applied Environmental Microbiology, 78:6295, 2012 : PubMed

            

    Title: Characterization of two metagenome-derived esterases that reactivate chloramphenicol by counteracting chloramphenicol acetyltransferase
    Tao W, Lee MH, Yoon MY, Kim JC, Malhotra S, Wu J, Hwang EC, Lee SW
    Ref: J Microbiol Biotechnol, 21:1203, 2011 : PubMed

            


Other Papers


Send your questions or comments to :
Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
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