NCBI Accession #
NP_563742.1
NCBI GenBank Nucleotide #
NM_100435.3
NCBI Official Full Name
UDP-glucosyltransferase 75B1
NCBI Official Symbol
UGT75B1
NCBI Official Synonym Symbols
T25N20.21; UDP-GLUCOSE TRANSFERASE 1; UDP-GLUCOSYLTRANSFERASE; UDP-glucosyltransferase 75B1; UGT1
NCBI Protein Information
UDP-glucosyltransferase 75B1
NCBI Summary
A UDP-glucose transferase localized in the phragmoplast. It has been co-purified with the callose synthase complex and may transfer UDP-glucose from sucrose synthase to the callose synthase and thus help form a substrate channel for the synthesis of callose at the forming cell plate. Induced by salicylic acid. Independent of NPR1 for their induction by salicylic acid. UGT1 encodes a protein with glucosyltransferase activity with high sequence homology to UGT2 (AT1G05530). It belongs to an UGT subfamily that binds UDP-glucose but not UDP-glucuronate, UDP-galactose, or UDP-rhamnose as the glycosyl donor. UGT1 was shown to be able to use abscisic acid as glycosylation substrate in the presence of UDP-glucose. UGT1/UGT75B1 catalyzes the formation of the p-aminobenzoate-glucose ester in vitro and in vivo. It appears to be the enzyme predominantly responsible for pABA-Glc formation in Arabidopsis based on assays in leaves, flowers, and siliques.
UniProt Gene Name
UGT75B1
UniProt Synonym Gene Names
UGT1
UniProt Protein Name
UDP-glycosyltransferase 75B1
UniProt Synonym Protein Names
(Uridine 5'-diphosphate-glucose:indol-3-ylacetyl)-beta-D-glucosyl transferase 1; IAA-Glu synthase 1; Indole-3-acetate beta-glucosyltransferase 1 (EC:2.4.1.121)
UniProt Primary Accession #
Q9LR44
UniProt Related Accession #
Q9LR44
UniProt Comments
Possesses low catalytic activity on indole-3-acetic acid (IAA) in vitro. May transfer UDP-glucose from sucrose synthase to callose synthase for the synthesis of callose at the forming cell plate during cytokinesis. Has high affinity for 4-aminobenzoate. Catalyzes the formation of 4-aminobenzoate glucose ester which represents a storage form of 4-aminobenzoate in the vacuole. Is the major source of this activity in the plant. Also active in vitro on benzoates and benzoate derivatives.