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Information on EC 2.7.7.9 - UTP-glucose-1-phosphate uridylyltransferase and Organism(s) Arabidopsis thaliana and UniProt Accession Q9M9P3
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2.7.7.9 UTP-glucose-1-phosphate uridylyltransferaseSpecify your search results
Word Map
- 2.7.7.9
- phosphoglucomutase
- polysaccharide
- glycogen
- galactose
- udp-galactose
- adp-glucose
- exopolysaccharide
- dictyostelium
- udp-sugars
- udp-n-acetylglucosamine
-
leloir
- galactose-1-phosphate
-
udp-glucuronic
- galactokinase
-
aureobasidium
-
pyrophosphorolysis
-
sucrose-phosphate
- gellan
- xylinum
- agriculture
- synthesis
- medicine
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
udp-glucose pyrophosphorylase, ugpase, udpg-pyrophosphorylase, udpgp, udp-glc pyrophosphorylase, udpglucose pyrophosphorylase, glucose-1-phosphate uridylyltransferase, udpg pyrophosphorylase, utp-glucose-1-phosphate uridylyltransferase, uridine diphosphoglucose pyrophosphorylase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
glucose 1-phosphate uridylyltransferase
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-
-
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glucose-1-phosphate uridylyltransferase
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-
-
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UDP glucose pyrophosphorylase
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-
-
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UDP-glucose pyrophosphorylase
UDPG phosphorylase
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-
-
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UDPG pyrophosphorylase
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-
-
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UDPglucose pyrophosphorylase
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-
-
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uridine 5'-diphosphoglucose pyrophosphorylase
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-
-
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uridine diphosphate-D-glucose pyrophosphorylase
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-
-
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uridine diphosphoglucose pyrophosphorylase
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-
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uridine-diphosphate glucose pyrophosphorylase
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-
-
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uridylyltransferase, glucose 1-phosphate
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-
-
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UDP-glucose pyrophosphorylase
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
nucleotidyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
KEGG
-
-, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
UTP:alpha-D-glucose-1-phosphate uridylyltransferase
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CAS REGISTRY NUMBER
COMMENTARY
9026-22-6
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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
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
-
-
?
UTP + alpha-D-glucose 1-phosphate
UDP-glucose + diphosphate
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
-
-
?
UTP + alpha-D-glucose 1-phosphate
UDP-glucose + diphosphate
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
UDP-glucose + diphosphate
Q94B70
14.2% activity with galactose-1-phosphate
-
-
?
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
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
-
-
?
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
diphosphate
Q94B70
with 0.25 mM 57% activity, with 1 mM 11% activity, with 10 mM 1.5% activity
additional information
structure-activity relationship of the salicylimide derived inhibitors
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
enzyme expression is inducible by exogenous sucrose, light and cold stress
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
the UGPase protein content and enzyme activity in the Pi-deficient mutant is about twice as high as in wild type and Pi-excess mutants, regardless of the light/dark conditions
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
UGP3 is a soluble plastid UDP-glucose pyrophosphorylase converts glucose-1-phosphate to UDP-glucose in the stroma
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
lack of sulfoquinovosyldiacylglycerol in the Arabidopsis ugp3 knockout mutant. The mutant does not show significant differences in glycosides and saccharides between wild type and ugp3 mutants
metabolism
physiological function
metabolism
-
the enzyme is important in sulfoquinovosyldiacylglycerol, SQDG, biosynthesis in chloroplasts together with UDP-sulfoquinovose synthase, SQD1 EC 3.13.1.1, and SQDG synthase, SQD2, mechanism for SQDG biosynthesis, overview. Sulfoquinovosyldiacylglycerol is the only sulfur-containing anionic glycerolipid, a relatively minor relatively minor, and is the least prevalent component of photosynthetic membrane lipids. The function of SQDG under phosphate-limited growth conditions is highly correlated with the regulation of other plant glycerolipid biosyntheses. UGP3 is not involved in the biosynthesis of secondary metabolites and cellulose, but rather is likely to be specifically involved in SQDG synthesis
metabolism
-
UGP2 is unable to replace UGP1 in the UGP1 knockout lines, even though it bears similar metabolic functions to UGP. The majority of proteins that are responsive to FB1 treatment are located in the chloroplast and have functions associated with photosynthesis
physiological function
-
the enzyme is a critical factor that regulates FB1-induced programmed cell death, an active form of cell suicide that is tightly regulated at the genetic level, only being activated when required, mechanism, overview
physiological function
-
UGP3 is a plastid UDP-glucose pyrophosphorylase that supplies UDP-glucose to UDP-sulfoquinovose synthase, SQD1, in plastids
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). UGPA2_ARATH
469
0
51738
Swiss-Prot
other Location (Reliability: 3)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
53000
53000, native PAGE and SDS-PAGE, calculated without His-tag: 51600 Da
53000
53000, native PAGE and SDS-PAGE, calculated without His-tag: 51700 Da
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
53000, native PAGE and SDS-PAGE, calculated without His-tag: 51600 Da
monomer
53000, native PAGE and SDS-PAGE, calculated without His-tag: 51700 Da
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
uncomplexed enzyme and in presence of UTP and UDP-glucose. Structures show a carboxy-terminal beta-helix domain in a unique orientation. The nucleotide binding loop and the carboxy-terminal domain, including the possible catalytically important K360, move in and out of the active site in a concerted fashion
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
construction of transgenic plants, with increased or deleted expression of enzyme, study of sucrose effects on the enzyme and gene Ugp, respectively
additional information
-
UGP2 is unable to replace UGP1 in UGP1 knockout lines
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
His-tagged version expressed in Escherichia coli BL21 (DE3)
His-tagged version expressed in Escherichia coli BL21 (DE3)
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ciereszko, I.; Johansson, H.; Kleczkowski, L.A.
Sucrose and light regulation of a cold-inducible UDP-glucose pyrophosphorylase gene via a hexokinase-independent and abscisic acid-insensitive pathway in Arabidopsis
Biochem. J.
354
67-72
2001
Arabidopsis thaliana
Ciereszko, I.; Johansson, H.; Kleczkowski, L.A.
Interactive effects of phosphate deficiency, sucrose and light/dark conditions on gene expression of UDP-glucose pyrophosphorylase in Arabidopsis
J. Plant Physiol.
162
343-353
2005
Arabidopsis thaliana
McCoy, J.G.; Bitto, E.; Bingman, C.A.; Wesenberg, G.E.; Bannen, R.M.; Kondrashov, D.A.; Phillips, G.N.
Structure and dynamics of UDP-glucose pyrophosphorylase from Arabidopsis thaliana with bound UDP-glucose and UTP
J. Mol. Biol.
366
830-841
2007
Arabidopsis thaliana (Q9M9P3), Arabidopsis thaliana
Siddique, S.; Endres, S.; Atkins, J.M.; Szakasits, D.; Wieczorek, K.; Hofmann, J.; Blaukopf, C.; Urwin, P.E.; Tenhaken, R.; Grundler, F.M.; Kreil, D.P.; Bohlmann, H.
Myo-inositol oxygenase genes are involved in the development of syncytia induced by Heterodera schachtii in Arabidopsis roots
New Phytol.
184
457-472
2009
Arabidopsis thaliana (P57751), Arabidopsis thaliana (Q9M9P3)
Meng, M.; Wilczynska, M.; Kleczkowski, L.A.
Molecular and kinetic characterization of two UDP-glucose pyrophosphorylases, products of distinct genes, from Arabidopsis
Biochim. Biophys. Acta
1784
967-972
2008
Arabidopsis thaliana (P57751), Arabidopsis thaliana (Q9M9P3)
Meng, M.; Geisler, M.; Johansson, H.; Harholt, J.; Scheller, H.V.; Mellerowicz, E.J.; Kleczkowski, L.A.
UDP-glucose pyrophosphorylase is not rate limiting, but is essential in Arabidopsis
Plant Cell Physiol.
50
998-1011
2009
Arabidopsis thaliana (P57751), Arabidopsis thaliana (Q94B70)
Okazaki, Y.; Shimojima, M.; Sawada, Y.; Toyooka, K.; Narisawa, T.; Mochida, K.; Tanaka, H.; Matsuda, F.; Hirai, A.; Hirai, M.Y.; Ohta, H.; Saito, K.
A chloroplastic UDP-glucose pyrophosphorylase from Arabidopsis is the committed enzyme for the first step of sulfolipid biosynthesis
Plant Cell
21
892-909
2009
Arabidopsis thaliana (Q94B70), Arabidopsis thaliana
Chivasa, S.; Tome, D.F.; Slabas, A.R.
UDP-glucose pyrophosphorylase is a novel plant cell death regulator
J. Proteome Res.
12
1743-1753
2013
Arabidopsis thaliana, Arabidopsis thaliana Col-0
Shimojima, M.
Biosynthesis and functions of the plant sulfolipid
Prog. Lipid Res.
50
234-239
2011
Arabidopsis thaliana, Spinacia oleracea
Decker, D.; Oeberg, C.; Kleczkowski, L.A.
Identification and characterization of inhibitors of UDP-glucose and UDP-sugar pyrophosphorylases for in vivo studies
Plant J.
90
1093-1107
2017
Arabidopsis thaliana (P57751), Arabidopsis thaliana (Q9M9P3), Hordeum vulgare (Q43772)
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