CSDB glycosyltransferase search

3 glycosyltransferase activities have 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: RfaC UniProt ID: P24173 CAZy family: GT9 Gene name: waaC / rfaC Gene GenBank ID: 948136*	Synthesized dimer: aLDmanHepp(1-5)aKdo Donor (ID 34402): bXLDmanHepp(1-P-P-5)xXnucA Acceptor (ID 34403): l?3HOMyr(1-2)[lXLau(1-3)l?3HOMyr(1-2)[aXKdo(2-4)aXKdo(2-6),P-4),lXMyr(1-3)l?3HOMyr(1-3)]bDGlcpN(1-6),l?3HOMyr(1-3)]aDGlcpN(1-P Status: evidence in vitro Confirmation methods: in vitro (crude extract), in vitro (purified protein), mutation (dual, rfaC + rfaF) ID: 2097 Notes: WaaA, WaaC, WaaF, and WaaQ participate in the synthesis of Ac(1-2)b?GlcpN(1-7)?XLDmanHepp(1-6)??Glcp(1-2)??Glcp(1-3)[??Gal?(1-6)]??Glcp(1-3)[?XLDmanHepp(1-7)]aXLDmanHepp(1-3)aXLDmanHepp(1-5)[<>[%xXEtN(1-7)]aXKdo(2-4)]aXKdo(2-6)[lXLau(1-3)l?3HOMyr(1-2),P-4),lXMyr(1-3)l?3HOMyr(1-3)]bDGlcpN(1-6)[l?3HOMyr(1-3),l?3HOMyr(1-2)]aDGlcpN(1-P.	Organism (ID 23): Escherichia coli K12 Full structure (ID 34404): Molecule role (analog of): core	Gronow et al. 2000 DOI: 10.1046/j.1432-1327.2000.01754.x Brabetz et al. 1997 DOI: 10.1111/j.1432-1033.1997.00716.x Grizon et al. 2006 DOI: 10.1016/j.jmb.2006.07.057 Gronow et al. 2001 DOI: 10.1177/09680519010070040701 Czyzyk et al. 2011 DOI: 10.1021/bi201581b
Synthesized dimer: aLDmanHepp(1-5)aKdo Donor (ID 34402): bXLDmanHepp(1-P-P-5)xXnucA Acceptor (ID 34405): l?3HOMyr(1-2)[l?3HOMyr(1-2)[aXKdo(2-4)aXKdo(2-6),P-4),l?3HOMyr(1-3)]bDGlcpN(1-6),l?3HOMyr(1-3)]aDGlcpN(1-P Status: evidence in vitro Confirmation methods: in vitro (crude extract) ID: 2098 Notes: WaaA, WaaC, WaaF, and WaaQ participate in the synthesis of Ac(1-2)b?GlcpN(1-7)?XLDmanHepp(1-6)??Glcp(1-2)??Glcp(1-3)[??Gal?(1-6)]??Glcp(1-3)[?XLDmanHepp(1-7)]aXLDmanHepp(1-3)aXLDmanHepp(1-5)[<>[%xXEtN(1-7)]aXKdo(2-4)]aXKdo(2-6)[lXLau(1-3)l?3HOMyr(1-2),P-4),lXMyr(1-3)l?3HOMyr(1-3)]bDGlcpN(1-6)[l?3HOMyr(1-3),l?3HOMyr(1-2)]aDGlcpN(1-P.	Organism (ID 23): Escherichia coli K12 Full structure (ID 34406): Molecule role (analog of): core	Gronow et al. 2000 DOI: 10.1046/j.1432-1327.2000.01754.x Gronow et al. 2001 DOI: 10.1177/09680519010070040701
Enzyme name: RfaC UniProt ID: P24173* CAZy family: GT9 Gene name: waaC / rfaC Gene GenBank ID: 948136*	Synthesized dimer: aLDmanHepp(1-5)aKdo Donor (ID 34402): bXLDmanHepp(1-P-P-5)xXnucA Acceptor (ID 34407): aXKdo(2-4)aXKdo(2-6)[P-4)]bDGlcpN(1-6)aDGlcpN(1-P Status: evidence in vitro Confirmation methods: in vitro (purified protein) ID: 2099	Organism (ID 16634): Escherichia coli K12 MB1760 Full structure (ID 34408):	Czyzyk et al. 2011 DOI: 10.1021/bi201581b

#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)
2097	RfaC				P24173		GT9	waaC / rfaC	948136	*		34404		l?3HOMyr(1-2)[lXLau(1-3)l?3HOMyr(1-2)[aXKdo(2-4)[aXLDmanHepp(1-5)]aXKdo(2-6),P-4),lXMyr(1-3)l?3HOMyr(1-3)]bDGlcpN(1-6),l?3HOMyr(1-3)]aDGlcpN(1-P	0	aXLDmanHepp(1-5)aXKdo?	4~5	bXLDmanHepp(1-P-P-5)xXnucA	l?3HOMyr(1-2)[lXLau(1-3)l?3HOMyr(1-2)[aXKdo(2-4)aXKdo(2-6),P-4),lXMyr(1-3)l?3HOMyr(1-3)]bDGlcpN(1-6),l?3HOMyr(1-3)]aDGlcpN(1-P	in vitro	in vitro (crude extract), in vitro (purified protein), mutation (dual, rfaC + rfaF)	WaaA, WaaC, WaaF, and WaaQ participate in the synthesis of Ac(1-2)b?GlcpN(1-7)?XLDmanHepp(1-6)??Glcp(1-2)??Glcp(1-3)[??Gal?(1-6)]??Glcp(1-3)[?XLDmanHepp(1-7)]aXLDmanHepp(1-3)aXLDmanHepp(1-5)[<>[%xXEtN(1-7)]aXKdo(2-4)]aXKdo(2-6)[lXLau(1-3)l?3HOMyr(1-2),P-4),lXMyr(1-3)l?3HOMyr(1-3)]bDGlcpN(1-6)[l?3HOMyr(1-3),l?3HOMyr(1-2)]aDGlcpN(1-P.	core	1	0			23	Escherichia coli K12		Gronow et al. 2000 (doi: 10.1046/j.1432-1327.2000.01754.x); Brabetz et al. 1997 (doi: 10.1111/j.1432-1033.1997.00716.x); Grizon et al. 2006 (doi: 10.1016/j.jmb.2006.07.057); Gronow et al. 2001 (doi: 10.1177/09680519010070040701); Czyzyk et al. 2011 (doi: 10.1021/bi201581b)	
2098	RfaC				P24173		GT9	waaC / rfaC	948136	*		34406		l?3HOMyr(1-2)[l?3HOMyr(1-2)[aXKdo(2-4)[aXLDmanHepp(1-5)]aXKdo(2-6),P-4),l?3HOMyr(1-3)]bDGlcpN(1-6),l?3HOMyr(1-3)]aDGlcpN(1-P	0	aXLDmanHepp(1-5)aXKdo?	4~5	bXLDmanHepp(1-P-P-5)xXnucA	l?3HOMyr(1-2)[l?3HOMyr(1-2)[aXKdo(2-4)aXKdo(2-6),P-4),l?3HOMyr(1-3)]bDGlcpN(1-6),l?3HOMyr(1-3)]aDGlcpN(1-P	in vitro	in vitro (crude extract)	WaaA, WaaC, WaaF, and WaaQ participate in the synthesis of Ac(1-2)b?GlcpN(1-7)?XLDmanHepp(1-6)??Glcp(1-2)??Glcp(1-3)[??Gal?(1-6)]??Glcp(1-3)[?XLDmanHepp(1-7)]aXLDmanHepp(1-3)aXLDmanHepp(1-5)[<>[%xXEtN(1-7)]aXKdo(2-4)]aXKdo(2-6)[lXLau(1-3)l?3HOMyr(1-2),P-4),lXMyr(1-3)l?3HOMyr(1-3)]bDGlcpN(1-6)[l?3HOMyr(1-3),l?3HOMyr(1-2)]aDGlcpN(1-P.	core	1	0			23	Escherichia coli K12		Gronow et al. 2000 (doi: 10.1046/j.1432-1327.2000.01754.x); Gronow et al. 2001 (doi: 10.1177/09680519010070040701)	
2099	RfaC				P24173	*	GT9	waaC / rfaC	948136	*		34408		aXKdo(2-4)[aXLDmanHepp(1-5)]aXKdo(2-6)[P-4)]bDGlcpN(1-6)aDGlcpN(1-P	0	aXLDmanHepp(1-5)aXKdo?	4~5	bXLDmanHepp(1-P-P-5)xXnucA	aXKdo(2-4)aXKdo(2-6)[P-4)]bDGlcpN(1-6)aDGlcpN(1-P	in vitro	in vitro (purified protein)			0	0			16634	Escherichia coli K12 MB1760		Czyzyk et al. 2011 (doi: 10.1021/bi201581b)