Gene_Locus Report

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Gene_locus Report for: 9bact-LAE6

Uncultured bacterium esterase LAE6 EH1 EH1AB1 alpha/beta hydrolase enzyme from the metagenome of Lake Arreo, Spain

Comment
EH1A promiscuous activity 72/96 substrates Martinez-Martinez et al. 2018 . Using Ser211 as nucleophile computationally designed additional mutations, adding Glu25Asp and Leu214His double mutant gives an additional active site with Gly207, Tyr208 and Phe209 act as a potential oxyanion hole Santiagoet al. 2018


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
5 structures (e.g. : 5JD4, 6I8D, 6I8F... more)
No kinetic





No Substrate
5 inhibitors (e.g. : 6RKY-K7K, B4-4NHP, Butoxyhexylphosphonate... more)
1 Genbank : SRA059294
>3 Structure links 2 more: 6I8F, 6RB0, 6RKY
Sequence
Graphical view for this peptide sequence: 9bact-LAE6
Colored MSA for Hormone-sensitive_lipase_like (raw)
MLLPETRNLLDLMDAATRGGRPRLETLPHAVGRKAVDKMSEDGEADPPEV
AEVANGGFAGPASEIRFRRYRPLGEAAGLLPTLIYYHGGGFVIGNIETHD
STCRRLANKSRCQVISIDYRLAPEHPFPAPIDDGIAAFRHIRDNAESFGA
DAARLAVGGDSAGGAMAAVVCQACRDAGETGPAFQMLIYPATDSSRESAS
RVAFAEGYFLSKALMDWFWEAYVPEDTDLTDLRLSPLLATDFTGLPPAFV
LTAGYDPLRDEGRAYADRLIEAGIKTTYVNYPGTIHGFFSLTRFLSQGLK
ANDEAAAVMGAHFGT
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

MLLPETRNLLDLMDAATRGGRPRLETLPHAVGRKAVDKMSEDGEADPPEV
AEVANGGFAGPASEIRFRRYRPLGEAAGLLPTLIYYHGGGFVIGNIETHD
STCRRLANKSRCQVISIDYRLAPEHPFPAPIDDGIAAFRHIRDNAESFGA
DAARLAVGGDSAGGAMAAVVCQACRDAGETGPAFQMLIYPATDSSRESAS
RVAFAEGYFLSKALMDWFWEAYVPEDTDLTDLRLSPLLATDFTGLPPAFV
LTAGYDPLRDEGRAYADRLIEAGIKTTYVNYPGTIHGFFSLTRFLSQGLK
ANDEAAAVMGAHFGT


References
1 more
    Title: Genetically engineered proteins with two active sites for enhanced biocatalysis and synergistic chemo- and biocatalysis
    Alonso S, Santiago G, Cea-Rama I, Fernandez-Lopez L, Coscolin C, Modregger J, Ressmann A, Martinez-Martinez M, Marrero H and Ferrer M <11 more author(s)>
    Ref: Nature Catalysis, 3:319, 2019 : PubMed

            

    Title: Determinants and prediction of esterase substrate promiscuity patterns
    Martinez-Martinez M, Coscolin C, Santiago G, Chow J, Stogios PJ, Bargiela R, Gertler C, Navarro-Fernandez J, Bollinger A and Ferrer M <32 more author(s)>
    Ref: ACS Chemical Biology, 13:225, 2018 : PubMed

            

    Title: Biochemical diversity of carboxyl esterases and lipases from lake arreo (Spain): a metagenomic approach
    Martinez-Martinez M, Alcaide M, Tchigvintsev A, Reva O, Polaina J, Bargiela R, Guazzaroni ME, Chicote A, Canet A and Ferrer M <4 more author(s)>
    Ref: Applied Environmental Microbiology, 79:3553, 2013 : 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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