Gene_Locus Report

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Gene_locus Report for: thefu-1831

Thermobifida fusca putative carboxylesterase TfCa

Comment
Other strains: Thermobifida fusca (Tfus_37; YX; KW3; TM51) Carboxylesterase TfCa


Relationship
Family|Carb_B_Bacteria
Block| C
Position in NCBI Life Tree|Thermobifida fusca
(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 > 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
Warning: This entry is a compilation of different species or line or strain with more than 90% amino acid identity. You can retrieve all strain data


Molecular evidence
Database
No mutation
4 structures (e.g. : 7W1I, 7W1J, 7W1K... more)
No kinetic





9 substrates (e.g. : 2PET, BECBA, BETEB... more)
1 inhbitor:
Phthalate
>3 Genbank links 1 more: NZ_AAAQ01000037, CP000088, FN401519
3 UniProt : Q47M62, P86325, C5JAB7
1 Ncbi-nid : 23018727
1 Ncbi-pid : 23018749
>3 Structure links 1 more: 7W1I, 7W1J, 7W1K
3 UniProt : Q47M62, P86325, C5JAB7
3 Interpro : Q47M62, P86325, C5JAB7
3 Pfam : Q47M62, P86325, C5JAB7
3 PIRSF : Q47M62, P86325, C5JAB7
3 SUPERFAM : Q47M62, P86325, C5JAB7
Sequence
Graphical view for this peptide sequence: thefu-1831
Colored MSA for Carb_B_Bacteria (raw)
MANEKSSRVPLDITHPALLGRNRLVGKERGKCVEIVIRTGSGDVRGSKEN
GIAVFRGIPYAEPPVGAHRFTAPRPPRPWDGVRDATEFSATAPRPPYPEA
IGALLIERFIPGDDYLTLNVWTPDPNAVGLPVMVWIHGGAFTNGSGSEPV
YDGAAFARDGVVFVSFNYRLGIIGFADLPDAPSNRGLLDQIAALEWVRDN
IARFGGDPGNVTVFGESAGAMSVCTLMATPRARGLFRRAILQSGAGNMAV
AAEDATTIAAVIAHRLGVEPTAAALAHVPVAQLLDVQQQVAQEIQGAPDP
AVWGERIAGGSVLLPFAPVIDGELLSQRPAEAIAGGAGHDVDLLFGTTTD
EYRLFLAPTGLLPFITGDYVTTHLAKSGLDADAAKAYTAEGRGEEPGDIL
ASIITDQVFRIPALRIAESRVDAPARTFGYEFAWRTPQLDGILGACHAVE
LPFVFRTLDRAASLVGTNPPEELAETVHNAWVRFATSGDPGWPAWNPETR
SVMRFDHPVSEMVTDPYPATRALWDGVPL
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

MANEKSSRVPLDITHPALLGRNRLVGKERGKCVEIVIRTGSGDVRGSKEN
GIAVFRGIPYAEPPVGAHRFTAPRPPRPWDGVRDATEFSATAPRPPYPEA
IGALLIERFIPGDDYLTLNVWTPDPNAVGLPVMVWIHGGAFTNGSGSEPV
YDGAAFARDGVVFVSFNYRLGIIGFADLPDAPSNRGLLDQIAALEWVRDN
IARFGGDPGNVTVFGESAGAMSVCTLMATPRARGLFRRAILQSGAGNMAV
AAEDATTIAAVIAHRLGVEPTAAALAHVPVAQLLDVQQQVAQEIQGAPDP
AVWGERIAGGSVLLPFAPVIDGELLSQRPAEAIAGGAGHDVDLLFGTTTD
EYRLFLAPTGLLPFITGDYVTTHLAKSGLDADAAKAYTAEGRGEEPGDIL
ASIITDQVFRIPALRIAESRVDAPARTFGYEFAWRTPQLDGILGACHAVE
LPFVFRTLDRAASLVGTNPPEELAETVHNAWVRFATSGDPGWPAWNPETR
SVMRFDHPVSEMVTDPYPATRALWDGVPL


References
5 more
    Title: Structural Insights into (Tere)phthalate-Ester Hydrolysis by a Carboxylesterase and Its Role in Promoting PET Depolymerization
    von Haugwitz G, Han X, Pfaff L, Li Q, Wei H, Gao J, Methling K, Ao Y, Brack Y and Wei R <11 more author(s)>
    Ref: ACS Catal, 12:15259, 2022 : PubMed

            

    Title: Perspectives on the Role of Enzymatic Biocatalysis for the Degradation of Plastic PET
    Magalhaes RP, Cunha JM, Sousa SF
    Ref: Int J Mol Sci, 22:11257, 2021 : PubMed

            

    Title: High level expression of a hydrophobic poly(ethylene terephthalate)-hydrolyzing carboxylesterase from Thermobifida fusca KW3 in Escherichia coli BL21(DE3)
    Oeser T, Wei R, Baumgarten T, Billig S, Follner C, Zimmermann W
    Ref: J Biotechnol, 146:100, 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.
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