Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.4.1.91 - flavonol 3-O-glucosyltransferase and Organism(s) Medicago truncatula and UniProt Accession Q5IFH7

for references in articles please use BRENDA:EC2.4.1.91
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     2 Transferases
         2.4 Glycosyltransferases
             2.4.1 Hexosyltransferases
                2.4.1.91 flavonol 3-O-glucosyltransferase
IUBMB Comments
Acts on a variety of flavonols, including quercetin and quercetin 7-O-glucoside. Different from EC 2.4.1.81 (flavone 7-O-beta-glucosyltransferase).
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Medicago truncatula
UNIPROT: Q5IFH7
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Medicago truncatula
The enzyme appears in selected viruses and cellular organisms
Synonyms
flavonoid 3-o-glucosyltransferase, ugt71g1, flavonoid-3-o-glucosyltransferase, flavonol 3-o-glucosyltransferase, flavonoid 3-o-glycosyltransferase, fagt6, fagt7, ugt706c1, ugt707a3, vl3gt, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
UDP flavonoid/triterpene GT
-
F3GT
-
-
-
-
glucosyltransferase, uridine diphosphoglucose-flavonol 3-O-
-
-
-
-
GT-I
-
-
-
-
GTI
-
-
-
-
UDP-glucose:flavonol 3-O-glucosyltransferase
-
-
-
-
UDPG:flavonoid-3-O-glucosyltransferase
-
-
-
-
UDPglucose:flavonol O3-D-glucosyltransferase
-
-
-
-
UFGT
-
-
-
-
additional information
the enzyme belongs to the UGT superfamily
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
UDP-glucose + a flavonol = UDP + a flavonol 3-O-beta-D-glucoside
show the reaction diagram
His22 acts as the catalytic base, and Asp121 is a key residue that may assist deprotonation of the acceptor by forming an electron transfer chain with the catalytic base, both residues, as well as Glu381, are essential in donor substrate binding and enzyme activity, acceptor substrate binding site structure
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexosyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
UDP-glucose:flavonol 3-O-D-glucosyltransferase
Acts on a variety of flavonols, including quercetin and quercetin 7-O-glucoside. Different from EC 2.4.1.81 (flavone 7-O-beta-glucosyltransferase).
CAS REGISTRY NUMBER
COMMENTARY hide
50812-18-5
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
UDP-alpha-D-glucose + quercetin
UDP + quercetin 3-O-beta-D-glucoside
show the reaction diagram
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
UDP-alpha-D-glucose + quercetin
UDP + quercetin 3-O-beta-D-glucoside
show the reaction diagram
-
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q5IFH7_MEDTR
465
0
51785
TrEMBL
-
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
wild-type and selenomethionine-labeled enzyme in complex with UDP and UDP-glucose, hanging drop vapour diffusion method, 5 mg/ml protein is mixed with 5 mM UDP-galactose and 5 mM quercetin at a 2:1 v/v ratio, mixed with an equal volume of reservoir solution containing 40% w/v PEG 3350, 0.2 M ammonium acetate, and 0.1 M sodium citrate, pH 5.6, equilibration over the reservoir solution at 20°C, 2-5 days, X-ray diffraction structure determination and analysis at 2.0-2.6 A resolution, molecular docking
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D121A
site-directed mutagenesis, inactive mutant
D121N
site-directed mutagenesis, inactive mutant
E381A
site-directed mutagenesis, inactive mutant
H22A
site-directed mutagenesis, inactive mutant
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, anion exchange chromatography, and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3), selenomethionine-labeled enzyme in Escherichia coli strain B834(DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Shao, H.; He, X.; Achnine, L.; Blount, J.W.; Dixon, R.A.; Wang, X.
Crystal structures of a multifunctional triterpene/flavonoid glycosyltransferase from Medicago truncatula
Plant Cell
17
3141-3154
2005
Medicago truncatula (Q5IFH7), Medicago truncatula
Manually annotated by BRENDA team