sacvd-c7mve8

 
Saccharomonospora viridis PET-degrading cutinase Cut190 SvCut190. Cutinase

Comment
Other strains: Saccharomonospora viridis (strain ATCC 15386 / DSM 43017 / JCM 3036 / NBRC 12207 / P101)


Relationship
Block L
Saccharomonospora viridis 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 > Pseudonocardiales: N E > Pseudonocardiaceae: N E > Saccharomonospora: N E > Saccharomonospora viridis: 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
11 structures (e.g. : 7CTR, 7CTS, 7CEF... more)
No kinetic

Substrate: Monoethyl-succinate , Monoethyl-adipate , Polyethylene-terephthalate ,

2 Genbank : CP001683, AB728484
2 UniProt : C7MVE8, W0TJ64
>3 Structure links 8 more: 7CTR, 7CTS, 7CEF
2 UniProtTrembl : C7MVE8, W0TJ64
2 Interpro : C7MVE8, W0TJ64
2 Prodom : C7MVE8, W0TJ64
2 Pfam : C7MVE8, W0TJ64
2 PIRSF : C7MVE8, W0TJ64
2 SUPERFAM : C7MVE8, W0TJ64
2 QuickSwissBlast : C7MVE8, W0TJ64
 
Sequence
Graphical view for this peptide sequence: sacvd-c7mve8
Colored MSA for Polyesterase-lipase-cutinase (raw)
MRIRRQAGTGARASMARAIGVMTTALAVLVGAVGGVAGAEVSTAQDNPYE
RGPDPTEDSIEAIRGPFSVATERVSSFASGFGGGTIYYPRETDEGTFGAV
AVAPGFTASQGSMSWYGERVASQGFIVFTIDTNTRLDQPGQRGRQLLAAL
DYLVERSDRKVRERLDPNRLAVMGHSMGGGGSLEATVMRPSLKASIPLTP
WNLDKTWGQVQVPTFIIGAELDTIASVRTHAKPFYESLPSSLPKAYMELD
GATHFAPNIPNTTIAKYVISWLKRFVDEDTRYSQFLCPNPTDRAIEEYRS
TCPY
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

MRIRRQAGTGARASMARAIGVMTTALAVLVGAVGGVAGAEVSTAQDNPYE
RGPDPTEDSIEAIRGPFSVATERVSSFASGFGGGTIYYPRETDEGTFGAV
AVAPGFTASQGSMSWYGERVASQGFIVFTIDTNTRLDQPGQRGRQLLAAL
DYLVERSDRKVRERLDPNRLAVMGHSMGGGGSLEATVMRPSLKASIPLTP
WNLDKTWGQVQVPTFIIGAELDTIASVRTHAKPFYESLPSSLPKAYMELD
GATHFAPNIPNTTIAKYVISWLKRFVDEDTRYSQFLCPNPTDRAIEEYRS
TCPY

no DNA




References
8 more
    Title: Structural basis of mutants of PET-degrading enzyme from Saccharomonospora viridis AHK190 with high activity and thermal stability
    Emori M, Numoto N, Senga A, Bekker GJ, Kamiya N, Kobayashi Y, Ito N, Kawai F, Oda M
    Ref: Proteins, 89:502, 2021 : PubMed

            

    Title: The Current State of Research on PET Hydrolyzing Enzymes Available for Biorecycling
    Kawai F
    Ref: Catalysts, 11:206, 2021 : PubMed

            

    Title: Structural basis for Ca(2+)-dependent catalysis of a cutinase-like enzyme and its engineering: application to enzymatic PET depolymerization
    Oda M
    Ref: Biophys Physicobiol, 18:168, 2021 : 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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