(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) > cellular organisms: NE > Bacteria: NE > FCB group: NE > Bacteroidetes/Chlorobi group: NE > Bacteroidetes: NE > Flavobacteriia: NE > Flavobacteriales: NE > Flavobacteriaceae: NE > Aequorivita: NE > Aequorivita viscosa: NE
LegendThis 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 MKIIYPLAVLFLITSLAPNTIFAQCEDVTIESLTNPGPYEVATLTEDDGI RNGPDYLDATVYYPTNATPPYASIAIVPGFTAQPSSVEEWGPFYASHGIV TIIIGTNSPFEFPDLRATALLDALETLRQENERQNSPLENQLDVDKFAVS GWSMGGGGAQLAAQMDSSIKAVLALCPWYPQATFNHNSPVLIFSGQDDTV APPGIHADVHYNVTPDTTNKLLFEVANGSHSVANTPTGGDGVVGKIALSW LKLYLDDNDCYCPLLTDSLLVDPPAASKVEASFECEPIIGIAENNIDISI
https://www.researchsquare.com/article/rs-567691/v2
Polyethylene terephthalate (PET) is an important synthetic polymer accumulating in nature 2 and recent studies have identified microorganisms capable of degrading PET. While the majority of 3 known PET hydrolases originate from the Actinobacteria and Proteobacteria, here we describe the 4 first functional PET-active enzymes from the Bacteroidetes phylum. Using a PETase-specific 5 Hidden-Markov-Model (HMM)-based search algorithm we identified two promiscuous and cold6 active esterases derived from Aequorivita sp. (PET27) and Chryseobacterium jeonii (PET30) acting 7 on PET foil and powder. Notably, one of the enzymes (PET30) was able to hydrolyze PET at 8 temperatures between 4 - 30 C with a similar turnover rate compared to the well-known Ideonella 9 sakaiensis enzyme (IsPETase). 10 PET27 and PET30 homologues were detected in metagenomes encompassing a wide range 11 of different global climate zones. Additional transcript abundance mapping of marine samples imply 12 that these promiscuous enzymes and source organisms may play a role in the long-term 13 degradation of microplastic particles and fibers.
