Summary: UDP-glucoronosyl and UDP-glucosyl transferase
This is the Wikipedia entry entitled "Glucuronosyltransferase". More...
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Glucuronosyltransferase Edit Wikipedia article
|PDB structures||RCSB PDB PDBe PDBsum|
|Gene Ontology||AmiGO / EGO|
|UDP-glucuronosyl and UDP-glucosyl transferase|
Structure of TDP-vancosaminyltransferase GtfD as a complex with TDP and the natural substrate, desvancosaminyl vancomycin.
Uridine 5'-diphospho-glucuronosyltransferase (UDP-glucuronosyltransferase, UGT) is a glycosyltransferase (EC 220.127.116.11) that catalyzes the transfer of the glucuronic acid component of UDP-glucuronic acid to a small hydrophobic molecule. This is a glucuronidation reaction.
- UDP-glucuronyl transferase
Glucuronosyltransferases are responsible for the process of glucuronidation, a major part of phase II metabolism. Arguably the most important of the Phase II (conjugative) enzymes, UGTs have been the subject of increasing scientific inquiry since the mid-to-late 1990s.
The reaction catalyzed by the UGT enzyme involves the addition of a glucuronic acid moiety to xenobiotics and is the most important pathway for the human body's elimination of the top 200 drugs. It is also the major pathway for foreign chemical (dietary, environmental, pharmaceutical) removal for most drugs, dietary substances, toxins and endogenous substances. UGT is present in humans, other animals, plants, and bacteria. Famously, UGT enzymes are not present in the genus Felis, and this accounts for a number of unusual toxicities in the cat family.
The glucuronidation reaction consists of the transfer of the glucuronosyl group from uridine 5'-diphospho-glucuronic acid (UDPGA) to substrate molecules that contain oxygen, nitrogen, sulfur or carboxyl functional groups. The resulting glucuronide is more polar (e.g. hydrophilic) and more easily excreted than the substrate molecule. The product solubility in blood is increased allowing it to be eliminated from the body by the kidneys.
It is also associated with Crigler-Najjar syndrome, a more serious disorder where the enzyme's activity is either completely absent (Crigler-Najjar syndrome type I) or less than 10% of normal (type II).
Infants may have a developmental deficiency in UDP-glucuronyl transferase, and are unable to hepatically metabolize the antibiotic drug chloramphenicol which requires glucuronidation. This leads to a condition known as gray baby syndrome.
Human genes which encode UGT enzymes include:
- B3GAT1, B3GAT2, B3GAT3
- UGT1A1, UGT1A3, UGT1A4, UGT1A5, UGT1A6, UGT1A7, UGT1A8, UGT1A9, UGT1A10
- UGT2A1, UGT2A2, UGT2A3, UGT2B4, UGT2B7, UGT2B10, UGT2B11, UGT2B15, UGT2B17, UGT2B28
- Mulichak AM, Lu W, Losey HC, Walsh CT, Garavito RM (May 2004). "Crystal structure of vancosaminyltransferase GtfD from the vancomycin biosynthetic pathway: interactions with acceptor and nucleotide ligands". Biochemistry 43 (18): 5170–5180. doi:10.1021/bi036130c. PMID 15122882.
- King C, Rios G, Green M, Tephly T (2000). "UDP-glucuronosyltransferases". Curr Drug Metab 1 (2): 143–161. doi:10.2174/1389200003339171. PMID 11465080.
- Court MH and Greenblatt DJ (2000). "Molecular genetic basis for deficient acetaminophen glucuronidation by cats: UGT1A6 is a pseudogene, and evidence for reduced diversity of expressed hepatic UGT1A isoforms". Pharmacogenetics. 10 (4): 355–69. doi:10.1097/00008571-200006000-00009. PMID 10862526.
- Bock K, Köhle C (2005). "UDP-glucuronosyltransferase 1A6: structural, functional, and regulatory aspects". Methods Enzymol 400: 57–75. doi:10.1016/S0076-6879(05)00004-2. PMID 16399343.
- MacDougall, C; Chambers, HF (2011). "55". Protein Synthesis Inhibitors and Miscellaneous Antibacterial Agents. In: Brunton LL, Chabner BA, Knollmann BC, eds. Goodman & Gilman's The Pharmacological Basis of Therapeutics. (12 ed.). New York: McGraw-Hill. Retrieved October 19, 2011.
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UDP-glucoronosyl and UDP-glucosyl transferase Provide feedback
No Pfam abstract.
Internal database links
|Similarity to PfamA using HHSearch:||Glyco_tran_28_C Glyco_trans_1_3|
External database links
This tab holds annotation information from the InterPro database.
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 (EC) (UDPGT) [PUBMED:1909870]. 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] (EC) (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). 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 (EC) [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 (EC) (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) [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.
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||transferase activity, transferring hexosyl groups (GO:0016758)|
|Biological process||metabolic process (GO:0008152)|
- the number of sequences which exhibit this architecture
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This is the GT-B clan that contains diverse glycosyltransferases that possess a Rossmann like fold .
The clan contains the following 35 members:Alg14 Capsule_synth DUF1205 DUF1972 DUF3492 DUF354 Epimerase_2 Glyco_tran_28_C Glyco_trans_1_2 Glyco_trans_1_3 Glyco_trans_1_4 Glyco_trans_4_2 Glyco_trans_4_3 Glyco_trans_4_4 Glyco_transf_20 Glyco_transf_28 Glyco_transf_4 Glyco_transf_41 Glyco_transf_5 Glyco_transf_56 Glyco_transf_9 Glyco_transf_90 Glycogen_syn Glycos_transf_1 Glycos_transf_N Glyphos_transf LpxB MGDG_synth Mito_fiss_Elm1 Phosphorylase PIGA PS_pyruv_trans SUA5 Sucrose_synth UDPGT
We make a range of alignments for each Pfam-A family:
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Curation and family details
|Number in seed:||14|
|Number in full:||8949|
|Average length of the domain:||279.00 aa|
|Average identity of full alignment:||18 %|
|Average coverage of the sequence by the domain:||62.32 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||13|
|Download:||download the raw HMM for this family|
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There is 1 interaction for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
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 25 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 seqence.
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