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: pmt1p UniProt ID: P33775* CAZy family: GT39 Gene name: PMT1 Gene GenBank ID: 851462*	Synthesized dimer: DMan(1-3)Ser Donor (ID 34645): ?DManp(1-P-1)Subst // Subst = dolichol Acceptor (ID 34653): Ac(1-2)/x?Ser?(1-2)/n=4/x?Ser? Status: evidence in vitro Confirmation methods: in vitro (microsomal membrane preparation); in vitro (purified protein) ID: 42 Notes: The exact position and degree of mannosylation is unknown. Overexpression of both pmt1p and pmt2p resulted in increased mannosyltransferase activity in vitro.	Organism (ID 10157): Saccharomyces cerevisiae SEY6210 Full structure (ID 34654): Molecule role (analog of): O-glycan	Gentzsch et al. 1995 DOI: 10.1016/0014-5793(95)01324-5 Gentzsch et al. 1997 DOI: 10.1093/glycob/7.4.481 Lommel et al. 2011 DOI: 10.1074/jbc.M111.281196 Immervoll et al. 1995 DOI: 10.1002/yea.320111403 Lussier et al. 1995b DOI: 10.1074/jbc.270.6.2770
Synthesized dimer: DMan(1-3)Ser Donor (ID 34645): ?DManp(1-P-1)Subst // Subst = dolichol Acceptor (ID 34653): Ac(1-2)/x?Ser?(1-2)/n=4/x?Ser? Status: evidence in vitro Confirmation methods: in vitro (membrane preparation), mutation ID: 73 Notes: Pmt3 forms a heterodimeric complex with PMT5 and more rarely with PMT1 to transfer mannose from Dol-P-mannose to Ser or Thr residues on proteins. PMT1 and PMT2 can compensate for a deleted PMT3 gene.	Organism (ID 10157,16758): Saccharomyces cerevisiae SEY6210, SEY6211 Full structure (ID 34654): CSDB ID(s): 40828 Molecule role (analog of): O-glycan	Gentzsch et al. 1997 DOI: 10.1093/glycob/7.4.481
Enzyme name: pmt2p UniProt ID: P31382* CAZy family: GT39 Gene name: PMT2 Gene GenBank ID: 851210*	Synthesized dimer: DMan(1-3)Ser Donor (ID 34645): ?DManp(1-P-1)Subst // Subst = dolichol Acceptor (ID 34653): Ac(1-2)/x?Ser?(1-2)/n=4/x?Ser? Status: evidence in vitro Confirmation methods: in vitro (membrane preparation), mutation ID: 82 Notes: Pmt3 forms a heterodimeric complex with PMT5 and more rarely with PMT1 to transfer mannose from Dol-P-mannose to Ser or Thr residues on proteins. PMT1 and PMT2 can compensate for a deleted PMT3 gene.	Organism (ID 10157,16758): Saccharomyces cerevisiae SEY6210, SEY6211 Full structure (ID 34654): CSDB ID(s): 40828 Molecule role (analog of): O-glycan

#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)
42	pmt1p				P33775	*	GT39	PMT1	851462	*		34654		Ac(1-2)x?Ser?(1-2)/[%?DMan(1-3)]x?Ser?(1-2)/n=3/[%?DMan(1-3)]x?Ser?	0	?DMan?(1-3)x?Ser?	1~3	?DManp(1-P-1)Subst // Subst = dolichol	Ac(1-2)/x?Ser?(1-2)/n=4/x?Ser?	in vitro	in vitro (microsomal membrane preparation); in vitro (purified protein)	The exact position and degree of mannosylation is unknown. Overexpression of both pmt1p and pmt2p resulted in increased mannosyltransferase activity in vitro.	O-glycan	1	0			10157	Saccharomyces cerevisiae SEY6210		Gentzsch et al. 1995 (doi: 10.1016/0014-5793(95)01324-5); Gentzsch et al. 1997 (doi: 10.1093/glycob/7.4.481); Lommel et al. 2011 (doi: 10.1074/jbc.M111.281196); Immervoll et al. 1995 (doi: 10.1002/yea.320111403); Lussier et al. 1995b (doi: 10.1074/jbc.270.6.2770)	
73	pmt1p				P33775	*	GT39	PMT1	851462	*		34654		Ac(1-2)x?Ser?(1-2)/[%?DMan(1-3)]x?Ser?(1-2)/n=3/[%?DMan(1-3)]x?Ser?	0	?DMan?(1-3)x?Ser?	1~3	?DManp(1-P-1)Subst // Subst = dolichol	Ac(1-2)/x?Ser?(1-2)/n=4/x?Ser?	in vitro	in vitro (membrane preparation), mutation	Pmt3 forms a heterodimeric complex with PMT5 and more rarely with PMT1 to transfer mannose from Dol-P-mannose to Ser or Thr residues on proteins. PMT1 and PMT2 can compensate for a deleted PMT3 gene.	O-glycan	1	0		40828	10157,16758	Saccharomyces cerevisiae SEY6210, SEY6211		Gentzsch et al. 1997 (doi: 10.1093/glycob/7.4.481)	
82	pmt2p				P31382	*	GT39	PMT2	851210	*		34654		Ac(1-2)x?Ser?(1-2)/[%?DMan(1-3)]x?Ser?(1-2)/n=3/[%?DMan(1-3)]x?Ser?	0	?DMan?(1-3)x?Ser?	1~3	?DManp(1-P-1)Subst // Subst = dolichol	Ac(1-2)/x?Ser?(1-2)/n=4/x?Ser?	in vitro	in vitro (membrane preparation), mutation	Pmt3 forms a heterodimeric complex with PMT5 and more rarely with PMT1 to transfer mannose from Dol-P-mannose to Ser or Thr residues on proteins. PMT1 and PMT2 can compensate for a deleted PMT3 gene.	O-glycan	1	0		40828	10157,16758	Saccharomyces cerevisiae SEY6210, SEY6211		Gentzsch et al. 1997 (doi: 10.1093/glycob/7.4.481)