16  structures 491  species 1  interaction 4173  sequences 35  architectures

Family: UDPGT (PF00201)

Summary

UDP-glucoronosyl and UDP-glucosyl transferase Add an annotation

No Pfam abstract.


InterPro entry IPR002213

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 () (UDPGT) PUBMED:1909870, PUBMED:. 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 PUBMED:7694285 () (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 (). An enzyme PUBMED: 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 () PUBMED:2505387 (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 () (gene crtX), an enzyme involved in carotenoid biosynthesis and that catalyses the glycosylation reaction which converts zeaxanthin to zeaxanthin-beta-diglucoside.
  • Streptomyces macrolide glycosyltransferases () PUBMED:8244027. 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.

Clan

This family is a member of clan GT-B (CL0113), which contains the following 19 members:

Alg14 Capsule_synth DUF1022 DUF1205 DUF354 Epimerase_2 Glyco_tran_28_C Glyco_transf_20 Glyco_transf_28 Glyco_transf_5 Glyco_transf_9 Glycogen_syn Glycos_transf_1 Glyphos_transf LpxB MGDG_synth Phosphorylase PS_pyruv_trans UDPGT

Gene Ontology

External database links

Domain organisation

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

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Alignments

There are various ways to view or download the sequence alignments that we store. You can use a sequence viewer to look at either the seed or full alignment for the family, or you can look at a plain text version of the sequence in a variety of different formats. More...

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Very large alignments can often cause problems for the formatting tool above. If you find that downloading or viewing a large alignment is problematic, you can also download a gzip-compressed, Stockholm-format file containing the seed or full alignment for this family.

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

The main seed and full alignments are generated using sequences from the UniProt sequence database. However, we also generate alignments using sequences from the NCBI sequence database and the "metaseq" metagenomics dataset.

You can view alignments from these two additional datasets using the form above, or you can download alignments of NCBI or metagenomics sequences, as gzip-compressed files.

Pfam alignments:
Full length sequences

External links

MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER2.

Pfam alignments:

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...

Trees

This page displays the phylogenetic tree for this family. 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 or full alignments.

Note: You can also download the data files for the seed, full, NCBI or metagenomics trees.

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
Author: Finn RD
Number in seed: 14
Number in full: 4173
Average length of the domain: 276.60 aa
Average identity of full alignment: 20 %
Average coverage of the sequence by the domain: 59.28 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 9421015 -E 1000 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: 501
Family (HMM) version: 11
Download: download the raw HMM for this family

Species distribution

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The tree shows the occurrence of this domain across different species. More...

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Interactions

There is 1 interaction for this family. More...

UDPGT

Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the MSD 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.

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