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Information on EC 2.4.1.173 - sterol 3beta-glucosyltransferase and Organism(s) Saccharomyces cerevisiae and UniProt Accession Q06321
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EC Tree
2.4.1.173 sterol 3beta-glucosyltransferaseIUBMB Comments
Not identical with EC 2.4.1.192 (nuatigenin 3beta-glucosyltransferase) or EC 2.4.1.193 (sarsapogenin 3beta-glucosyltransferase).
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Word Map
- 2.4.1.173
- glucoside
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steryl
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glucosylation
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pexophagy
- somnifera
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withania
-
glucosyltransferases
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withanolide
- stigmasterol
- synthesis
- sitosterol
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3beta-hydroxy
- orbiculare
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udp-glucose-dependent
- udpase
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withaferin
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
sterol glucosyltransferase, atg26, ugt80b1, ugt80a2, sgtl1, ugt51, udpg-sgtase, sterol glycosyltransferase, sgtl2, udp-glucose:sterol glucosyltransferase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ScAtg26
multidomain protein which possesses pleckstrin homology, GRAM (glucosyltransferase, Rab-like GTPase activators, and myotubularins), and catalytic UDP-glucosyl transferase, domains
sterol glucosyltransferase
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sterol-beta-D-glucosyltransferase
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sterol:UDPG glucosyltransferase
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UDP-glucose-sterol beta-glucosyltransferase
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UDP-glucose-sterol glucosyltransferase
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UDPG-SGTase
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UDPG:sterol glucosyltransferase
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UDPglucose:sterol glucosyltransferase
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uridine diphosphoglucose-poriferasterol glucosyltransferase
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uridine diphosphoglucose-sterol glucosyltransferase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
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PATHWAY SOURCE
PATHWAYS
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-, -
SYSTEMATIC NAME
IUBMB Comments
UDP-glucose:sterol 3-O-beta-D-glucosyltransferase
Not identical with EC 2.4.1.192 (nuatigenin 3beta-glucosyltransferase) or EC 2.4.1.193 (sarsapogenin 3beta-glucosyltransferase).
CAS REGISTRY NUMBER
COMMENTARY
123940-38-5
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9075-00-7
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UDP-alpha-D-glucose + testosterone
UDP + testosterone 17-beta-D-glucoside
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-
-
?
UDP-glucose + estradiol
UDP + estradiol 3-beta-D-glucoside
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-
-
?
UDP-glucose + estrone
UDP + estrone 3-beta-D-glucoside
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-
-
?
UDP-glucose + protopanaxadiol
UDP + protopanaxadiol 3-beta-D-glucoside
an unnatural substrate of enzyme mutant 7_1
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-
?
UDP-glucose + sitosterol
UDP + sitosterol 3-beta-D-glucoside
cloned enzyme glucosylates sitosterol
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?
UDP-glucose + stigmasterol
UDP + stigmasterol 3-beta-D-glucoside
cloned enzyme glucosylates stigmasterol
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?
UDP-glucose + tomatidine
UDP + tomatidine 3-beta-glucoside
cloned enzyme glucosylates tomatidine
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?
UDP-glucose + a sterol
UDP + a sterol 3-beta-D-glucoside
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-
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?
UDP-glucose + cholesterol
UDP + cholesterol 3-beta-D-glucoside
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-
-
?
UDP-glucose + cholesterol
UDP + cholesterol 3-beta-D-glucoside
cloned enzyme glucosylates cholesterol
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?
UDP-glucose + ergosterol
UDP + ergosterol 3-beta-D-glucoside
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-
-
?
UDP-glucose + ergosterol
UDP + ergosterol 3-beta-D-glucoside
cloned enzyme glucosylates ergosterol
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?
additional information
?
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UDP-glucose best glucose donor, CDP-glucose, GDP-glucose and UDP-xylopyranose are used but at significantly lower rates and UDP-mannose, UDP-glucaronic acid, GDP-mannose and TDP-glucose are not effective glucose donor
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?
additional information
?
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UDP-glucose best glucose donor, CDP-glucose, GDP-glucose and UDP-xylopyranose are used but at significantly lower rates and UDP-mannose, UDP-glucaronic acid, GDP-mannose and TDP-glucose are not effective glucose donor
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?
additional information
?
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experimental results suggest that the enzyme is not involved in the cytoplasm to vacuole targeting pathway, macroautophagy and pexophagy
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-
?
additional information
?
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experimental results suggest that the enzyme is not involved in the cytoplasm to vacuole targeting pathway, macroautophagy and pexophagy
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?
additional information
?
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substrate molecular docking and structure analysis of wild-type and mutant enzymes, sugar donor binding mechanism of UGT51, overview
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additional information
?
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substrate molecular docking and structure analysis of wild-type and mutant enzymes, sugar donor binding mechanism of UGT51, overview
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UDP-glucose + a sterol
UDP + a sterol 3-beta-D-glucoside
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-
-
?
additional information
?
-
experimental results suggest that the enzyme is not involved in the cytoplasm to vacuole targeting pathway, macroautophagy and pexophagy
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-
?
additional information
?
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experimental results suggest that the enzyme is not involved in the cytoplasm to vacuole targeting pathway, macroautophagy and pexophagy
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
UGT51 is not involved in autophagy-related pathways in Saccharomyces cerevisiae
physiological function
additional information
evolution
enzyme UGT51 is a member of the GT1 family, GT-B fold group, comprising two Rossman-like domains
physiological function
the membrane-bound enzyme, UDP-glucose:sterol glucosyltransferase, controls the steryl glycoside synthesis
physiological function
sterol glycosyltransferases (SGTs) catalyze the formation of a variety of glycosylated sterol derivatives and are involved in producing a plethora of bioactive natural products. Sterol glycosyltransferases as members of UGTs are involved in transferring a sugar from UDP-sugar to various SGs metabolites, including hormones and secondary metabolites
additional information
a long hydrophobic cavity, 9.2 A in width and 17.6 A in length located at the N-terminal domain of UGT51, is suitable for the accommodation of sterol acceptor substrates. A short, conserved sequence of S847-M851 is identified at the bottom of the hydrophobic cavity, which might be the steroid binding site and play an important role for the UGT51 catalytic specificity towards sterols. Molecular docking simulations revealing the sugar acceptor specificity, overview. The N- and C-terminal domains predominantly dictate acceptor and donor specificities, respectively. The donor substrate binds in a deep inter-domain pocket and a hydrophobic crevice on the surface of the N-terminal domain, which is proposed to be the binding site of the aglycone substrate
additional information
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a long hydrophobic cavity, 9.2 A in width and 17.6 A in length located at the N-terminal domain of UGT51, is suitable for the accommodation of sterol acceptor substrates. A short, conserved sequence of S847-M851 is identified at the bottom of the hydrophobic cavity, which might be the steroid binding site and play an important role for the UGT51 catalytic specificity towards sterols. Molecular docking simulations revealing the sugar acceptor specificity, overview. The N- and C-terminal domains predominantly dictate acceptor and donor specificities, respectively. The donor substrate binds in a deep inter-domain pocket and a hydrophobic crevice on the surface of the N-terminal domain, which is proposed to be the binding site of the aglycone substrate
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
UGT51 forms a dimer in solution. The dimeric structure of UGT51 has two subunits packed against each other in a parallel fashion and adopts a butterfly shape. The full length of UGT51 contain 1198 amino acids, which can be divided into several domains: pleckstrin homology (PH) domain, GRAM domain and catalytic domain. The PH domain responsible interact with membrane lipids, the GRAM domain is essential for proper protein association with its target membrane, while the catalytic domain is essentiell for synthesis steroid glycosides. Each subunit displays the typical GT-B fold of GTs, comprising two distinct N- and C-terminal Rossman-fold domains having a similar topology and connected by a linker peptide and a long C-terminal helix. The N-terminal domain, a seven-stranded parallel beta-sheet flanked by nine alpha-helices, and the C-terminal domain, a six-stranded beta-sheet surrounded by five alpha-helices, are assumed to bind the aglycone and the nucleotide-sugar donor, respectively. The C-terminal helices alpha7 (residues 1129-1144) and alpha8 (residues 1147-1171) cross and interact with each Rossman-fold domain
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant UGT51 alone and in complex with UDP-glucose, hanging drop vapor diffusion method, mixing of 20 mg/ml protein in 20 mM Tris-HCl, 500 mM NaCl, and 2 mM DTT, with reservoir solution containing 0.2 M ammonium acetate, 0.1 M HEPES, pH 7.5, 25% w/v PEG 3350 for the free enzyme, or containing 0.2 M MgCl2, 0.1 M Tris, pH 8.5, and 25% w/v PEG 3350 for the enzyme complex, receiving microcrystals, optimized crystallization protocol involves dispensing 0.0015 ml of 20 mg/ml protein and 0.001 ml of reservoir solution (containing 0.2 M MgCl2, 0.1 M Tris pH 8.5 and 25% w/v PEG 3350) and 500 nl of 0.001 diluted crystal seed stock solution, rod protein crystals appear after 3 days, 14°C, crystals are soaked in cryoprotectant solution with 5 mM UDP-glucose, X-ray diffraction structure determination and analysis at 2.77 A and 1.9 A resolutions, respectively, molecular replacement using the structure of GtfD (PDB ID 1rrv) as the search model, modeling
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
S801A/L802A/V804A/K812A/E816K/S849A/N892D
site-directed mutagenesis, the changed unique interaction network in mutant M7_1 with an 1800fold activity improvement toward an unnatural substrate protopanaxadiol (PPD), might influence its substrate preference
additional information
additional information
null mutant by deletion of ugt52 gene with no enzyme activity
additional information
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null mutant by deletion of ugt52 gene with no enzyme activity
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant N-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3)
recombinant N-terminally His6-tagged UGT51 residues 722-1198 Escherichia coli srain BL21(DE3) CodonPlus by nickel affinity chromatography, tag cleavage by thrombin, followed by a secons step of nickel affinity chromatography, gel filtration, and ultrafiltration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene AGT26, recombinant expression of N-terminally His6-tagged UGT51 residues 722-1198 from pET28a vector with a thrombin cleavage site in Escherichia coli srain BL21(DE3) CodonPlus
gene ATG26, DNA and amino acid sequence determination and analysis, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Warnecke, D.; Erdmann, R.; Fahl, A.; Hube, B.; Muller, F.; Zank, T.; Zahringer, U.; Heinz, E.
Cloning and functional expression of UGT genes encoding sterol glucosyltransferases from Saccharomyces cerevisiae, Candida albicans, Pichia pastoris, and Dictyostelium discoideum
J. Biol. Chem.
274
13048-13059
1999
Avena sativa (O22678), Avena sativa ugt80A1 (O22678), Candida albicans (Q5A950), Candida albicans, Dictyostelium discoideum (Q54IL5), Dictyostelium discoideum, Dictyostelium discoideum ugt52 (Q54IL5), Komagataella pastoris, Komagataella pastoris (Q9Y751), Komagataella pastoris GS115 (Q9Y751), Saccharomyces cerevisiae (Q06321), Saccharomyces cerevisiae
Cao, Y.; Klionsky, D.J.
Atg26 is not involved in autophagy-related pathways in Saccharomyces cerevisiae
Autophagy
3
17-20
2007
Saccharomyces cerevisiae (Q06321), Saccharomyces cerevisiae
Chaturvedi, P.; Mishra, M.; Akhtar, N.; Gupta, P.; Mishra, P.; Tuli, R.
Sterol glycosyltransferases-identification of members of gene family and their role in stress in Withania somnifera
Mol. Biol. Rep.
39
9755-9764
2012
Saccharomyces cerevisiae (Q06321)
Malik, V.; Zhang, M.; Dover, L.G.; Northen, J.S.; Flinn, A.; Perry, J.J.; Black, G.W.
Sterol 3beta-glucosyltransferase biocatalysts with a range of selectivities, including selectivity for testosterone
Mol. Biosyst.
9
2816-2822
2013
Debaryomyces hansenii (Q6BN88), Debaryomyces hansenii CBS 767 (Q6BN88), Kluyveromyces lactis (Q6CUV2), Kluyveromyces lactis DSM 70799 (Q6CUV2), Komagataella pastoris (Q9Y751), Komagataella pastoris GS115 (Q9Y751), Meyerozyma guilliermondii (A5DNB9), Meyerozyma guilliermondii DSM 6381 (A5DNB9), Ogataea angusta (A7KAK6), Ogataea angusta DSM 70277 (A7KAK6), Saccharomyces cerevisiae (Q06321), Saccharomyces cerevisiae ATCC 204508 (Q06321)
Chen, L.; Zhang, Y.; Feng, Y.
Structural dissection of sterol glycosyltransferase UGT51 from Saccharomyces cerevisiae for substrate specificity
J. Struct. Biol.
204
371-379
2018
Saccharomyces cerevisiae (Q06321), Saccharomyces cerevisiae, Saccharomyces cerevisiae ATCC 204508 (Q06321)
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