CSDB glycosyltransferase search

1 glycosyltransferase activity has been found.
Please note that CSDB GT database covers only a few species: Arabidopsis thaliana, Escherichia coli, Saccharomyces cerevisiae, Acinetobacter baumannii.

Enzyme / Gene	Activity	Object	References
Enzyme name: 89A2 UniProt ID: Q9LZD8.1 CAZy family: GT1 Gene name: AT5G03490 Gene GenBank ID: 831823	Synthesized dimer: DGlcp(1-?)2,3HOBz Donor (ID 33557): ?DGlcp(1-P-P-5)xXnucU Acceptor (ID 34009): xX2,3HOBz // 2,3HOBz = 2,3-dihydroxybenzoic acid Status: evidence in vitro Confirmation methods: in vitro (purified protein) ID: 1636 Notes: UGT89A2 from Col-0 is highly selective toward UDP-xylose as the sugar donor, and the isoform from C24 can utilize both UDP-glucose and UDP-xylose but with a higher affinity to the glucose donor.	Organism (ID 16625): Arabidopsis thaliana C24 Full structure (ID 34011):	Chen, Li 2017 DOI: 10.1111/tpj.13271

#GTR ID	Enzyme name	Enzyme group	Enzyme Genbank ID	Derived ID mark	Enzyme Uniprot ID	Derived ID mark	CAZY family	Gene name	Gene Genbank ID	Derived ID mark	Gene cluster	Full structure CSDB structure ID	Side product CSDB structure ID	Full structure	Full structure is fragment (0|1)	Synthesized bond	Synthesized bond location (from root ~ subst position)	Donor structure ID	Substrate structure	Confirmation status	Methods used	Notes	Molecule role	Molecule is a model of role (0|1)	Molecule is a precursor of role (0|1)	Main CSDB record ID	Additional CSDB record IDs	CSDB organism IDs	Organism names	Organs and tissues	References (;-separated)
1636	89A2				Q9LZD8.1		GT1	AT5G03490	831823			34011		?DGlcp(1-?)xX2,3HOBz // 2,3HOBz = 2,3-dihydroxybenzoic acid	0	?DGlcp(1-?)xX2,3HOBz?	1~?	?DGlcp(1-P-P-5)xXnucU	xX2,3HOBz // 2,3HOBz = 2,3-dihydroxybenzoic acid	in vitro	in vitro (purified protein)	UGT89A2 from Col-0 is highly selective toward UDP-xylose as the sugar donor, and the isoform from C24 can utilize both UDP-glucose and UDP-xylose but with a higher affinity to the glucose donor.		0	0			16625	Arabidopsis thaliana C24		Chen, Li 2017 (doi: 10.1111/tpj.13271)