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: KpsS UniProt ID: P42218*	Synthesized dimer: bKdo(2-3)DGro Donor (ID 34590): bXKdo(2-P-5)xXnucC Acceptor (ID 34597): lXPam(1-3)[xDGro(1-P-1)]xDGro Status: evidence in vitro Confirmation methods: in vitro (purified protein); in vitro (deletion) ID: 2323 Notes: The E. coli KpsC enzyme possesses two GT active sites. The N-terminal GT (KpsC-NEc) is a β-(2→4)-Kdo transferase, whereas the C-terminal GT (KpsC-CEc) transfers β-(2→7)-linked Kdo residues12, creating the alternating linkages seen in the natural product.	Organism (ID 22): Escherichia coli Full structure (ID 34598):	Doyle et al. 2019 DOI: 10.1038/s41589-019-0276-8

#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)
2323	KpsS				P42218	*						34598		lXPam(1-3)[bXKdo(2-3)xDGro(1-P-1)]xDGro	0	bXKdo?(2-3)xDGro?	3~3	bXKdo(2-P-5)xXnucC	lXPam(1-3)[xDGro(1-P-1)]xDGro	in vitro	in vitro (purified protein); in vitro (deletion)	The E. coli KpsC enzyme possesses two GT active sites. The N-terminal GT (KpsC-NEc) is a β-(2→4)-Kdo transferase, whereas the C-terminal GT (KpsC-CEc) transfers β-(2→7)-linked Kdo residues12, creating the alternating linkages seen in the natural product.		1	0			22	Escherichia coli 		Doyle et al. 2019 (doi: 10.1038/s41589-019-0276-8)