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InterPro: IPR002213 UDP-glucuronosyl/UDP-glucosyltransferase

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UniProtKB

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5107 proteins

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Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
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Architectures
Accession List
Matches in BioMart

Accession

IPR002213 UDP_glucos_trans

Type

Family

Signatures Help

Database	ID	Name	Proteins
Pfam	PF00201	UDPGT	3992
PROSITE pattern	PS00375	UDPGT	2433
PANTHER	PTHR11926	UDP_glucos_trans	5039
Signatures in BioMart

InterPro Relationships Help

Children

IPR006326 UDP-glycosyltransferase, MGT
IPR016224 Ecdysteroid UDP-glucosyltransferase

GO Term annotation Help

Process

GO:0008152 metabolic process

Function

GO:0016758 transferase activity, transferring hexosyl groups

InterPro annotation

Entry Details in BioMart

Abstract

UDP glycosyltransferases (UGT) are a superfamily of enzymes that catalyzes the addition of the glycosyl group from a UTP-sugar to a small hydrophobic molecule. This family currently consist of:

Mammalian UDP-glucuronosyl transferases (EC:2.4.1.17) (UDPGT) [1, 2]. A large family of membrane-bound microsomal enzymes which catalyze the transfer of glucuronic acid to a wide variety of exogenous and endogenous lipophilic substrates. These enzymes are of major importance in the detoxification and subsequent elimination of xenobiotics such as drugs and carcinogens.
A large number of putative UDPGT from Caenorhabditis elegans.
Mammalian 2-hydroxyacylsphingosine 1-beta-galactosyltransferase [3] (EC:2.4.1.45) (also known as UDP-galactose-ceramide galactosyltransferase). This enzyme catalyzes the transfer of galactose to ceramide, a key enzymatic step in the biosynthesis of galactocerebrosides, which are abundant sphingolipids of the myelin membrane of the central nervous system and peripheral nervous system.
Plants flavonol O(3)-glucosyltransferase (EC:2.4.1.91). An enzyme [4] that catalyzes the transfer of glucose from UDP-glucose to a flavanol. This reaction is essential and one of the last steps in anthocyanin pigment biosynthesis.
Baculoviruses ecdysteroid UDP-glucosyltransferase (EC:2.4.1) [5] (egt). This enzyme catalyzes the transfer of glucose from UDP-glucose to ectysteroids which are insect molting hormones. The expression of egt in the insect host interferes with the normal insect development by blocking the molting process.
Prokaryotic zeaxanthin glucosyltransferase (EC:2.4.1) (gene crtX), an enzyme involved in carotenoid biosynthesis and that catalyses the glycosylation reaction which converts zeaxanthin to zeaxanthin-beta-diglucoside.
Streptomyces macrolide glycosyltransferases (EC:2.4.1) [6]. These enzymes specifically inactivates macrolide anitibiotics via 2'-O-glycosylation using UDP-glucose.

These enzymes share a conserved domain of about 50 amino acid residues located in their C-terminal section.

Structural links Help

PDB - click here

SCOP: c.87.1.10 , c.87.1.5

CATH: 3.40.50.2000

Database links Help

PDBe-motif: PS00375

Enzyme: EC:2.4.1

PROSITE doc: PDOC00359

PANDIT: PF00201

Blocks: IPB002213

Pfam Clan: CL0113.9

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR002213

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P16662 UDP-glucuronosyltransferase 2B7

P17717 UDP-glucuronosyltransferase 2B5

P34317 Putative UDP-glucuronosyltransferase ugt-60

Q53685 Oleandomycin glycosyltransferase

Q9M156 Probable hydroquinone glucosyltransferase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR007235	Glycosyl transferase, family 28, C-terminal
IPR002213	UDP-glucuronosyl/UDP-glucosyltransferase
IPR006326	UDP-glycosyltransferase, MGT
IPR004276	Glycosyl transferase, family 28
	SWISS-MODEL
	PDB Chain
	ModBase
	SCOP Domain

Publications Open in usermanual
1.	Burchell B, Nebert DW, Nelson DR, Bock KW, Iyanagi T, Jansen PL, Lancet D, Mulder GJ, Chowdhury JR, Siest G. The UDP glucuronosyltransferase gene superfamily: suggested nomenclature based on evolutionary divergence. DNA Cell Biol. 10 487-94 1991 [PubMed: 1909870]
2.	Dutton GJ. 1-78 1980
3.	Schulte S, Stoffel W. Ceramide UDPgalactosyltransferase from myelinating rat brain: purification, cloning, and expression. Proc. Natl. Acad. Sci. U.S.A. 90 10265-9 1993 [PubMed: 7694285] http://www.pubmedcentral.nih.gov/picrender.fcgi?tool=EBI&pubmedid=7694285&action=stream&blobtype=pdf
4.	Furtek D, Schiefelbein JW, Johnston F, Nelson OEJr. Sequence comparisons of 3 wild-type bronze-1 alleles from Zea mays. Plant Mol. Biol. 11 473-81 1988
5.	O'Reilly DR, Miller LK. A baculovirus blocks insect molting by producing ecdysteroid UDP-glucosyl transferase. Science 245 1110-2 1989 [PubMed: 2505387] http://www.sciencemag.org/cgi/content/abstract/245/4922/1110
6.	Hernandez C, Olano C, Mendez C, Salas JA. Characterization of a Streptomyces antibioticus gene cluster encoding a glycosyltransferase involved in oleandomycin inactivation. Gene 134 139-40 1993 [PubMed: 8244027] http://dx.doi.org/10.1016/0378-1119(93)90189-A

Additional Reading Open in usermanual
	Shao H, He X, Achnine L, Blount JW, Dixon RA, Wang X. Crystal structures of a multifunctional triterpene/flavonoid glycosyltransferase from Medicago truncatula. Plant Cell 17 2005 3141-54 [PubMed: 16214900] http://dx.doi.org/10.1105/tpc.105.035055
	Brazier-Hicks M, Offen WA, Gershater MC, Revett TJ, Lim EK, Bowles DJ, Davies GJ, Edwards R. Characterization and engineering of the bifunctional N- and O-glucosyltransferase involved in xenobiotic metabolism in plants. Proc. Natl. Acad. Sci. U.S.A. 104 2007 20238-43 [PubMed: 18077347] http://dx.doi.org/10.1073/pnas.0706421104
	Offen W, Martinez-Fleites C, Yang M, Kiat-Lim E, Davis BG, Tarling CA, Ford CM, Bowles DJ, Davies GJ. Structure of a flavonoid glucosyltransferase reveals the basis for plant natural product modification. EMBO J. 25 2006 1396-405 [PubMed: 16482224] http://dx.doi.org/10.1038/sj.emboj.7600970
	Mulichak AM, Lu W, Losey HC, Walsh CT, Garavito RM. Crystal structure of vancosaminyltransferase GtfD from the vancomycin biosynthetic pathway: interactions with acceptor and nucleotide ligands. Biochemistry 43 2004 5170-80 [PubMed: 15122882] http://dx.doi.org/10.1021/bi036130c

InterPro 23.1