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128  structures 3030  species 0  interactions 42599  sequences 485  architectures

Family: UDPGT (PF00201)

Summary: UDP-glucoronosyl and UDP-glucosyl transferase

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

Glucuronosyltransferase Edit Wikipedia article

EC number2.4.1.17
CAS number9030-08-4
IntEnzIntEnz view
ExPASyNiceZyme view
MetaCycmetabolic pathway
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
UDP-glucuronosyl and UDP-glucosyl transferase
PDB 1rrv EBI.jpg
Structure of TDP-vancosaminyltransferase GtfD as a complex with TDP and the natural substrate, desvancosaminyl vancomycin.[1]

Uridine 5'-diphospho-glucuronosyltransferase (UDP-glucuronosyltransferase, UGT) is a microsomal glycosyltransferase (EC that catalyzes the transfer of the glucuronic acid component of UDP-glucuronic acid to a small hydrophobic molecule. This is a glucuronidation reaction.[2][3]

Alternative names:

  • glucuronyltransferase
  • UDP-glucuronyl transferase
  • UDP-GT


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 most frequently prescribed 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,[4] 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.[5] 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.


A deficiency in the bilirubin specific form of glucuronosyltransferase is thought to be the cause of Gilbert's syndrome, which is characterized by unconjugated hyperbilirubinemia.

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.[6]


Causes of unconjugated hyperbilirubinemia are divided into three main categories, namely, excessive bilirubin synthesis, liver bilirubin uptake malfunction, and bilirubin conjugation compromise.[7]

As to excessive bilirubin synthesis, both intravascular hemolysis and extravascular hemolysis can involve in the pathophysiology.[7] Additionally, dyserythropoiesis and extravasation of blood into tissues such as angioedema and edema can also lead to indirect hyperbilirubinemia, along with heart failure, medication-induced, ethinyl estradiol, chronic hepatitis, and cirrhosis that are, otherwise, attributed to hepatic bilirubin mal-uptake and bilirubin conjugation compromise, respectively.[7]


Human genes which encode UGT enzymes include:


  1. ^ 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.
  2. ^ King C, Rios G, Green M, Tephly T (2000). "UDP-glucuronosyltransferases". Curr Drug Metab. 1 (2): 143–161. doi:10.2174/1389200003339171. PMID 11465080.
  3. ^ "UDP-glucuronosyltransferase 1-1". Drugbank. Retrieved 21 November 2019.
  4. ^ Court MH; 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.
  5. ^ 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.
  6. ^ 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.
  7. ^ a b c Namita Roy-Chowdhury, PhD, FAASLDJayanta Roy-Chowdhury, MD, MRCP, AGAF, FAASLD. "Diagnostic approach to the adult with jaundice or asymptomatic hyperbilirubinemia". UpToDate. Section Editor:Sanjiv Chopra, MD, MACPDeputy Editor:Shilpa Grover, MD, MPH, AGAF. Retrieved 2019-07-17.CS1 maint: uses authors parameter (link) CS1 maint: others (link)

External links

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

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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.
  • (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.
  • Streptomyces macrolide glycosyltransferases ( EC ) [ PUBMED:8244027 ]. These enzymes specifically inactivate macrolide antibiotics via 2'-O-glycosylation using UDP-glucose.

Gene Ontology

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Seed source: Prosite
Previous IDs: none
Type: Family
Sequence Ontology: SO:0100021
Author: Finn RD
Number in seed: 13
Number in full: 42599
Average length of the domain: 242.00 aa
Average identity of full alignment: 19 %
Average coverage of the sequence by the domain: 52.22 %

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HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 57096847 -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: 20
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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 128 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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