thefu-q6a0i4

 
Thermobifida fusca (Thermomonospora fusca), Thermobifida cellulosilytica; Thermobifida alba; Thermomyces cellullosylitic; Burkholderia cepacia Cutinase 2, Thc_Cut1 a; TfCut1 Tfu_0883 Tha_Cut1 Thf42_Cut1 Tfu_0883 TfHCut TfCut_2 (Cut2-kw3) FsCut

Comment
Other strains: Thermobifida fusca (Thermomonospora fusca)(DSM43793DSM44342, Thermobifida cellulosilytica DSM44535; Thermobifida alba DSM43185; Burkholderia cepacia (Pseudomonas cepacia)


Relationship
Block L
Thermobifida fusca YX position in NCBI Life Tree :
N link to NCBI taxonomic web page and E link to ESTHER gene locus found in this strain.
> cellular organisms: N E > Bacteria: N E > Terrabacteria group: N E > Actinobacteria [phylum]: N E > Actinobacteria [class]: N E > Streptosporangiales: N E > Nocardiopsaceae: N E > Thermobifida: N E > Thermobifida fusca: N E > Thermobifida fusca YX: 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
6 structures (e.g. : 7XTU, 5ZOA, 5LUI... more)
No kinetic

Substrate: ETETETE , TETET , EMT , EBT , Polyethylene-2,5-furandicarboxylate , BETE , BETEB , MHET , BHET , Polyurethane , Polyethylene-terephthalate , PBAT ,
Inhibitor: MHET , PMSF ,
>3 Genbank links 8 more: AAZ54921, WP_011291330, AET05799
>3 UniProt links 5 more: Q6A0I4, Q47RJ6, J7FDJ1
>3 Structure links 3 more: 7XTU, 5ZOA, 5LUI
>3 UniProtTrembl links 5 more: Q6A0I4, Q47RJ6, E9LVH7
>3 Interpro links 5 more: Q6A0I4, Q47RJ6, E9LVH7
>3 Prodom links 5 more: Q6A0I4, Q47RJ6, E9LVH7
>3 Pfam links 5 more: Q6A0I4, Q47RJ6, E9LVH7
>3 PIRSF links 5 more: Q6A0I4, Q47RJ6, E9LVH7
>3 SUPERFAM links 5 more: Q6A0I4, Q47RJ6, E9LVH7
>3 QuickSwissBlast links 5 more: Q6A0I4, Q47RJ6, E9LVH7
 
Sequence
Graphical view for this peptide sequence: thefu-q6a0i4
Colored MSA for Polyesterase-lipase-cutinase (raw)
MAVMTPRRERSSLLSRALQVTAAAATALVTAVSLAAPAHAANPYERGPNP
TDALLEASSGPFSVSEENVSRLSASGFGGGTIYYPRENNTYGAVAISPGY
TGTEASIAWLGERIASHGFVVITIDTITTLDQPDSRAEQLNAALNHMINR
ASSTVRSRIDSSRLAVMGHSMGGGGTLRLASQRPDLKAAIPLTPWHLNKN
WSSVTVPTLIIGADLDTIAPVATHAKPFYNSLPSSISKAYLELDGATHFA
PNIPNKIIGKYSVAWLKRFVDNDTRYTQFLCPGPRDGLFGEVEEYRSTCP
F
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

MAVMTPRRERSSLLSRALQVTAAAATALVTAVSLAAPAHAANPYERGPNP
TDALLEASSGPFSVSEENVSRLSASGFGGGTIYYPRENNTYGAVAISPGY
TGTEASIAWLGERIASHGFVVITIDTITTLDQPDSRAEQLNAALNHMINR
ASSTVRSRIDSSRLAVMGHSMGGGGTLRLASQRPDLKAAIPLTPWHLNKN
WSSVTVPTLIIGADLDTIAPVATHAKPFYNSLPSSISKAYLELDGATHFA
PNIPNKIIGKYSVAWLKRFVDNDTRYTQFLCPGPRDGLFGEVEEYRSTCP
F

no DNA




References
14 more
    Title: Comparative molecular docking and molecular-dynamic simulation of wild-type- and mutant carboxylesterase with BTA-hydrolase for enhanced binding to plastic
    Lameh F, Baseer AQ, Ashiru AG
    Ref: Eng Life Sciences, 22:13, 2022 : PubMed

            

    Title: Adsorption of enzymes with hydrolytic activity on polyethylene terephthalate
    Badino SF, Baath JA, Borch K, Jensen K, Westh P
    Ref: Enzyme Microb Technol, 152:109937, 2021 : PubMed

            

    Title: Substrate specificities of cutinases on aliphatic-aromatic polyesters and on their model substrates
    Perz V, Bleymaier K, Sinkel C, Kueper U, Bonnekessel M, Ribitsch D, Guebitz GM
    Ref: N Biotechnol, 33:295, 2016 : 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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