The December 2024 update of CAZy
The CAZy database introduces CAZac, a new, powerful and searchable descriptor of CAZyme reactions to complement the EC number system. Implemented for glycoside hydrolases, glycoside phosphorylases, transglycosidases, polysaccharide lyases and lytic polysaccharide monooxygenases, CAZac allows complex searches in the CAZy database to uncover the evolution of substrate specificity and mechanisms of CAZymes across families. publication here.
This month, we released one novel GT family, GT138 which rhamnosylate the plant protein RIN4 , following the publication by Peng and coworkers.
We wish you a merry Christmas and restful holidays and as said in South of France bon bout d’an !
CAZy now offers a platform facility that provides either automatic annotation or human curation services for your data.
The fully automatic annotation, is to provide users with high quality and most up-to-date results.
However, since automatic annotation is never error-free, and while we are working at constantly improving our pipeline, a "human curation" service also exists for the highest-quality analyses.
Because human curation requires expertise and time, and because such resources are limited, a query for human curation will have to be validated by the CAZy scientific committee.
If you are interested, please visit CAZy bioinformatics web page and contact : cazy@univ-amu.fr.
The CAZy database describes the families of structurally-related catalytic and carbohydrate-binding modules (or functional domains) of enzymes that degrade, modify, or create glycosidic bonds.
Online since 1998, CAZy is a specialist database dedicated to the display and analysis of genomic, structural and biochemical information on Carbohydrate-Active Enzymes (CAZymes).
CAZy data are accessible either by browsing sequence-based families or by browsing the content of genomes in carbohydrate-active enzymes. New genomes are added regularly shortly after they appear in the daily releases of GenBank. New families are created based on published evidence for the activity of at least one member of the family and all families are regularly updated, both in content and in description.
An original aspect of the CAZy database is its attempt to cover all carbohydrate-active enzymes across organisms and across subfields of glycosciences. Please let us know if some families have escaped our attention, we will be happy to add them !
For a more extensive encyclopedic resource on the particular features of carbohydrate active enzymes, please visit CAZypedia, a web site driven by the scientific community that studies these enzymes.
PULDB is a database of Polysaccharide Utilization Loci (PULs) in Bacteroidetes. PULDB displays information on experimentally determined and predicted PULs for a number of Bacteroidetes genomes.
A new reference for the CAZy database : We summarized the recent changes in the CAZy database, and evolution during the last eight years in an article published the Nucleic Acids Research (Database Issue), with a specific focus on functional annotations.
Read the full paper.
Enzyme Classes currently covered
Modules that catalyze the breakdown, biosynthesis or modification of carbohydrates and glycoconjugates :
– Glycoside Hydrolases (GHs) : hydrolysis and/or rearrangement of glycosidic bonds (see CAZypedia definition)
– GlycosylTransferases (GTs) : formation of glycosidic bonds (see definition)
– Polysaccharide Lyases (PLs) : non-hydrolytic cleavage of glycosidic bonds
– Carbohydrate Esterases (CEs) : hydrolysis of carbohydrate esters
– Auxiliary Activities (AAs) : redox enzymes that act in conjunction with CAZymes.
Associated Modules currently covered
Carbohydrate-active enzymes often display a modular structure with non-catalytic modules appended to the enzymes above
– Carbohydrate-Binding Modules (CBMs) : adhesion to carbohydrates
Genome analysis by CAZy
Family distribution and/or protein listings of the carbohydrate-active enzymes and associated proteins identified in genomes
– Genomes by Kingdom :
Last Functions released
a-L-arabinopyranosidase (AbpBs; BKA19_1748) | RZU32059.1 WP_104529000.1 | 3.2.1.- | pubmed |
b-glucosidase (MS614; MTS1_00907) | GAD33557.1 WP_023951833.1 | 3.2.1.21 | pubmed |
b-glucosidase (AS637) | WP_043484882.1 | 3.2.1.21 | pubmed |
b-glucosidase (CS617) | WP_020076619.1 | 3.2.1.21 | pubmed |
b-glucosidase (KA611; N801_16290) | KGN40173.1 WP_035939434.1 | 3.2.1.21 | pubmed |
b-glucosidase (CV626) | GGM89013.1 WP_030201081.1 | 3.2.1.21 | pubmed |
b-glucosidase (IB608) | WP_026862722.1 | 3.2.1.21 | pubmed |
b-glucosidase (TS608) | WP_020141869.1 | 3.2.1.21 | pubmed |
xylanase (XlnC; GCM10018777_00010) | GHF93985.1 | 3.2.1.8 | pubmed |
UDP-bLRhap: Thr-Rhamnosyl transferase (avirulence protein avrB) | AAA25726.1 | 2.4.1.- | pubmed |
b-xylosidase (Xyl43; PDE_06306) | EPS31351.1 | 3.2.1.37 | pubmed |
exo-b-1,3-glucosidase (CapGH3a;HUK09_00030) | MCF0235112.1 | 3.2.1.58 | pubmed |
MLG endo-b-1,4-glucosidase (CapGH16_3;HUK09_00025) | MCF0235111.1 | 3.2.1.- | pubmed |
glucan exo-b-1,3-glucosidase (CapGH3b;HUK09_00040) | MCF0235114.1 | 3.2.1.58 | pubmed |
b-xylosidase / a-L-arabinofuranosidase (CMU13 N1089) | CUN22903.1 WP_032850723.1 | 3.2.1.37 3.2.1.55 | pubmed pubmed |