Gene_Locus Report

Biblio print

Add to basket

Go to basket

Tree Display

AceDB Schema

XML Display

Feedback

Gene_locus Report for: 9psed-l7pyq2

Pseudomonas sp. ECU1011 Alpha/beta hydrolase fold-3 domain protein rPPE01

Relationship
Family|Hormone-sensitive_lipase_like
Block| H
Position in NCBI Life Tree|Pseudomonas sp. ECU1011
(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 > Proteobacteria: N E > Gammaproteobacteria: N E > Pseudomonadales: N E > Pseudomonadaceae: N E > Pseudomonas: N E > Pseudomonas sp. ECU1011: N E


Molecular evidence
Database
No mutation
5 structures (e.g. : 4OB6, 4OB7, 4OB8... more)
No kinetic





2 substrates: (S)-AcO-CPA, 2-acetyloxy-2-(2-chlorophenyl)acetate
No inhibitor
1 Genbank : JX679867
1 UniProt : L7PYQ2
>3 Structure links 2 more: 4OB6, 4OU4, 4OU5
1 UniProt : L7PYQ2
1 Interpro : L7PYQ2
1 Pfam : L7PYQ2
1 PIRSF : L7PYQ2
1 SUPERFAM : L7PYQ2
Sequence
Graphical view for this peptide sequence: 9psed-l7pyq2
Colored MSA for Hormone-sensitive_lipase_like (raw)
GSPGVEQHTKAFLEALEQGGGKPLEQLSPKDARAVLTGAQASVKVDLSGI
EVKERTIQANGQSIKLQVVRPANVKGELPVFMFFHGGGWVLGDFPTHQRL
IRDLVVGSGAVAVYVDYTPSPESHYPTAINQAYAATQWVAEHGKEIGVDG
KRLAVAGNSVGGNMAAVVALKAKEAGTPALRFQLLLWPVTDASFETASYK
QFADGHFLTTGMMKWFWDNYTTDAKAREQIYASPLRASSEQLKGLPPALV
QTAEFDVLRDEGEAYARKLNAAGVTVTSVRYNGMIHDYGLLNPLSQVPAV
KAAMRQAGTELKVHLQ
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

GSPGVEQHTKAFLEALEQGGGKPLEQLSPKDARAVLTGAQASVKVDLSGI
EVKERTIQANGQSIKLQVVRPANVKGELPVFMFFHGGGWVLGDFPTHQRL
IRDLVVGSGAVAVYVDYTPSPESHYPTAINQAYAATQWVAEHGKEIGVDG
KRLAVAGNSVGGNMAAVVALKAKEAGTPALRFQLLLWPVTDASFETASYK
QFADGHFLTTGMMKWFWDNYTTDAKAREQIYASPLRASSEQLKGLPPALV
QTAEFDVLRDEGEAYARKLNAAGVTVTSVRYNGMIHDYGLLNPLSQVPAV
KAAMRQAGTELKVHLQ


References
3 more
    Title: C-Terminal beta8-alpha9 Interaction Modulates Thermal Stability and Enzymatic Activity Differently in Hyperthermophilic Esterase EstE1 and Mesophilic Esterase rPPE
    Nguyen TA, Jang SH, Lee C
    Ref: Applied Environmental Microbiology, :e0066223, 2023 : PubMed

            

    Title: Crystal structures of Pseudomonas putida esterase reveal the functional role of residues 187 and 287 in substrate binding and chiral recognition
    Dou S, Kong XD, Ma BD, Chen Q, Zhang J, Zhou J, Xu JH
    Ref: Biochemical & Biophysical Research Communications, 446:1145, 2014 : PubMed

            

    Title: Bioproduction of chiral mandelate by enantioselective deacylation of alpha-acetoxyphenylacetic acid using whole cells of newly isolated Pseudomonas sp. ECU1011
    Ju X, Yu HL, Pan J, Wei DZ, Xu JH
    Ref: Applied Microbiology & Biotechnology, 86:83, 2010 : 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.
For technical information about these pages see:
ESTHER Home Page and ACEDB Home Page
AcePerl Lincoln Stein Home Page
webmaster

Acknowledgements and disclaimer