Gene_Locus Report

Biblio print

Add to basket

Go to basket

Tree Display

AceDB Schema

XML Display

Feedback

Gene_locus Report for: psepu-clcd1

Pseudomonas putida Pseudomonas sp. B13 dienelactone hydrolase clcD gene

Relationship
Family|Dienelactone_hydrolase
Block| X
Position in NCBI Life Tree|Pseudomonas putida
(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 putida group: N E > Pseudomonas putida: 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
18 structures (e.g. : 1DIN, 1GGV, 1ZI6... more)
No kinetic





1 substrate:
Dienelactone
1 inhbitor:
PMSF
>3 Genbank links 1 more: M15201, M16964, AF019038
3 UniProt : Q706U2, P0A115, P0A114
3 Ncbi-nid : 151136, 141915, 2444262
3 Ncbi-pid : 151137, 141918, 2444264
>3 Structure links 15 more: 1DIN, 1GGV, 4U2B
3 UniProt : Q706U2, P0A115, P0A114
3 Interpro : Q706U2, P0A115, P0A114
3 Prodom : Q706U2, P0A115, P0A114
3 Pfam : Q706U2, P0A115, P0A114
3 PIRSF : Q706U2, P0A115, P0A114
3 SUPERFAM : Q706U2, P0A115, P0A114
Sequence
Graphical view for this peptide sequence: psepu-clcd1
Colored MSA for Dienelactone_hydrolase (raw)
MLTEGISIQSYDGHTFGALVGSPAKAPAPVIVIAQEIFGVNAFMRETVSW
LVDQGYAAVCPDLYARQAPGTALDPQDERQREQAYKLWQAFDMEAGVGDL
EAAIRYARHQPYSNGKVGLVGYCLGGALAFLVAAKGYVDRAVGYYGVGLE
KQLKKVPEVKHPALFHMGGQDHFVPAPSRQLITEGFGANPLLQVHWYEEA
GHSFARTSSSGYVASAAALANERRLDFLAPLQSKKP
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

MLTEGISIQSYDGHTFGALVGSPAKAPAPVIVIAQEIFGVNAFMRETVSW
LVDQGYAAVCPDLYARQAPGTALDPQDERQREQAYKLWQAFDMEAGVGDL
EAAIRYARHQPYSNGKVGLVGYCLGGALAFLVAAKGYVDRAVGYYGVGLE
KQLKKVPEVKHPALFHMGGQDHFVPAPSRQLITEGFGANPLLQVHWYEEA
GHSFARTSSSGYVASAAALANERRLDFLAPLQSKKP


References
13 more
    Title: Substrate-induced activation of dienelactone hydrolase: an enzyme with a naturally occurring Cys-His-Asp triad
    Cheah E, Austin C, Ashley GW, Ollis D
    Ref: Protein Engineering, 6:575, 1993 : PubMed

            

    Title: Refined structure of dienelactone hydrolase at 1.8 A
    Pathak D, Ollis D
    Ref: Journal of Molecular Biology, 214:497, 1990 : PubMed

            

    Title: X-ray crystallographic structure of dienelactone hydrolase at 2.8 A
    Pathak D, Ngai KL, Ollis D
    Ref: Journal of Molecular Biology, 204:435, 1988 : 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