Protein
Thc_Cut1
ID: 28
Plastics: PBAT, PET, PLA
Organism: Thermobifida cellulosilytica DSM44535
Phylum: Actinomycetota
External organism resources: NCBI Taxonomy
Sequence length: 265
Verified activity: Yes
Sequence:
>28 Thc_Cut1 MANPYERGPNPTDALLEASSGPFSVSEENVSRLSASGFGGGTIYYPRENNTYGAVAISPG YTGTEASIAWLGERIASHGFVVITIDTITTLDQPDSRAEQLNAALNHMINRASSTVRSRI DSSRLAVMGHSMGGGGTLRLASQRPDLKAAIPLTPWHLNKNWSSVTVPTLIIGADLDTIA PVATHAKPFYNSLPSSISKAYLELDGATHFAPNIPNKIIGKYSVAWLKRFVDNDTRYTQF LCPGPRDGLFGEVEEYRSTCPFALE
External databases
UniProtKB
E9LVH8UniRef50
UniRef50_Q6A0I4UniRef90
UniRef90_Q6A0I4UniRef100
UniRef100_E9LVH8UniParc
UPI0001F734C7EMBL
ADV92526.1AlphaFold
E9LVH8PDB
5LUIReferences:
- Herrero Acero et al., 2011 — Enzymatic Surface Hydrolysis of PET: Effect of Structural Diversity on Kinetic Properties of Cutinases from Thermobifida
- Perz et al., 2016 — Substrate specificities of cutinases on aliphatic–aromatic polyesters and on their model substrates
- Ribitsch et al., 2017 — Small cause, large effect: Structural characterization of cutinases from Thermobifida cellulosilytica