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135  structures 3156  species 0  interactions 47187  sequences 499  architectures

Family: UDPGT (PF00201)

Summary: UDP-glucoronosyl and UDP-glucosyl transferase

Pfam includes annotations and additional family information from a range of different sources. These sources can be accessed via the tabs below.

This is the Wikipedia entry entitled "Glucuronosyltransferase". More...

Glucuronosyltransferase Edit Wikipedia article

The human uridine 5'-diphospho-glucuronosyltransferase (UDP-glucuronosyltransferase, UGT) enzymes catalyse the glucuronidation reaction, which consists to the transfer of the glucuronosyl group from uridine 5'-diphospho-glucuronic acid (UDPGA) to active endogenous and exogenous molecules with oxygen, nitrogen, sulfur or carboxyl functional groups. The resulting glucuronide products are more polar, generally water soluble, less toxic and more easily excreted than the substrate molecules. In humans, 18 proteins were characterized and categorized into two major families, UGT1 and UGT2 according to their primary amino acid sequence homology.

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

UDP-glucoronosyl and UDP-glucosyl transferase Provide feedback

No Pfam abstract.

Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR002213

UDP glycosyltransferases (UGT) are a superfamily of enzymes that catalyses 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 ) (UDPGT) [ PUBMED:1909870 ]. A large family of membrane-bound microsomal enzymes which catalyse 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. These enzymes are also involved in cancer progression and drug resistance [ PUBMED:32047295 ].
  • A large number of putative UDPGT from Caenorhabditis elegans.
  • Mammalian 2-hydroxyacylsphingosine 1-beta-galactosyltransferase [ PUBMED:7694285 ] ( EC ) (also known as UDP-galactose-ceramide galactosyltransferase). This enzyme catalyses 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 ), an enzyme that catalyses the transfer of glucose from UDP-glucose to a flavanol. This reaction is essential and one of the last steps in anthocyanin pigment biosynthesis. Gallate 1-beta-glucosyltransferase ( EC ), a glucosyltransferase that catalyses the formation of 1-O-galloyl-beta-D-glucose, the first committed step of hydrolyzable tannins (HTs) biosynthesis [ PUBMED:27227328 ].
  • (R)-mandelonitrile beta-glucosyltransferase from almond, which is involved in the biosynthesis of the cyanogenic glycoside (R)-prunasin (stereo-selective), a precursor of (R)-amygdalin which at high concentrations is associated with bitterness in kernels of almond [ PUBMED:32688778 ].
  • Baculoviruses ecdysteroid UDP-glucosyltransferase ( EC ) [ PUBMED:2505387 ] (egt). This enzyme catalyses 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 ) (gene crtX), an enzyme involved in carotenoid biosynthesis and that catalyses the glycosylation reaction which converts zeaxanthin to zeaxanthin-beta-diglucoside; Enterobactin C-glucosyltransferase iroB which catalyses the successive monoglucosylation, diglucosylation and triglucosylation of enterobactin decreasing the membrane affinity of Enterobactin and increasing the iron acquisition rate [ PUBMED:24960592 , PUBMED:17163637 ].
  • Streptomyces macrolide glycosyltransferases ( EC ) [ PUBMED:8244027 ]. These enzymes specifically inactivate macrolide antibiotics via 2'-O-glycosylation using UDP-glucose.

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets and the UniProtKB sequence database. More...

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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

Representative proteomes UniProt
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Representative proteomes UniProt

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We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

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You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

HMM logo

HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...


This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

Note: You can also download the data file for the tree.

Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: Prosite
Previous IDs: none
Type: Family
Sequence Ontology: SO:0100021
Author: Finn RD
Number in seed: 13
Number in full: 47187
Average length of the domain: 248.6 aa
Average identity of full alignment: 19 %
Average coverage of the sequence by the domain: 53.71 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 19.5 19.5
Trusted cut-off 19.5 19.5
Noise cut-off 19.4 19.4
Model length: 499
Family (HMM) version: 21
Download: download the raw HMM for this family

Species distribution

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Colour assignments

Archea Archea Eukaryota Eukaryota
Bacteria Bacteria Other sequences Other sequences
Viruses Viruses Unclassified Unclassified
Viroids Viroids Unclassified sequence Unclassified sequence


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This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. More...

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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the UDPGT domain has been found. There are 135 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.

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AlphaFold Structure Predictions

The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.

Protein Predicted structure External Information
A0A044QX37 View 3D Structure Click here
A0A061AKV1 View 3D Structure Click here
A0A077YVV2 View 3D Structure Click here
A0A077YX48 View 3D Structure Click here
A0A077Z0C4 View 3D Structure Click here
A0A077Z0Y1 View 3D Structure Click here
A0A077Z3D9 View 3D Structure Click here
A0A077Z4K4 View 3D Structure Click here
A0A077Z5C4 View 3D Structure Click here
A0A077Z5U4 View 3D Structure Click here
A0A077Z8K7 View 3D Structure Click here
A0A077Z8L2 View 3D Structure Click here
A0A077ZDR2 View 3D Structure Click here
A0A077ZFK0 View 3D Structure Click here
A0A096S680 View 3D Structure Click here
A0A096SRM5 View 3D Structure Click here
A0A0D1CFF0 View 3D Structure Click here
A0A0D2DDF0 View 3D Structure Click here
A0A0D2E5Q6 View 3D Structure Click here
A0A0D2EY87 View 3D Structure Click here
A0A0D2GYD3 View 3D Structure Click here
A0A0G2K4R2 View 3D Structure Click here
A0A0G4DBR5 View 3D Structure Click here
A0A0K0DTD6 View 3D Structure Click here
A0A0K0DU70 View 3D Structure Click here
A0A0K0DVP2 View 3D Structure Click here
A0A0K0DWJ7 View 3D Structure Click here
A0A0K0DWL0 View 3D Structure Click here
A0A0K0DXZ4 View 3D Structure Click here
A0A0K0DZR7 View 3D Structure Click here
A0A0K0E2S8 View 3D Structure Click here
A0A0K0E2X9 View 3D Structure Click here
A0A0K0E3C0 View 3D Structure Click here
A0A0K0E3T1 View 3D Structure Click here
A0A0K0E3T4 View 3D Structure Click here
A0A0K0E426 View 3D Structure Click here
A0A0K0E427 View 3D Structure Click here
A0A0K0E428 View 3D Structure Click here
A0A0K0E429 View 3D Structure Click here
A0A0K0E489 View 3D Structure Click here