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Information on EC 2.4.1.12 - cellulose synthase (UDP-forming) and Organism(s) Arabidopsis thaliana and UniProt Accession Q94JQ6

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EC Tree
     2 Transferases
         2.4 Glycosyltransferases
             2.4.1 Hexosyltransferases
                2.4.1.12 cellulose synthase (UDP-forming)
IUBMB Comments
Involved in the synthesis of cellulose. A similar enzyme utilizes GDP-glucose [EC 2.4.1.29 cellulose synthase (GDP-forming)].
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This record set is specific for:
Arabidopsis thaliana
UNIPROT: Q94JQ6
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Word Map
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The enzyme appears in selected viruses and cellular organisms
Synonyms
cellulose synthase, glucan synthase, cesa3, cellulose synthase complex, cesa6, cesa1, cesa7, csld3, cellulose synthase a, cesa4, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1,4-beta-D-glucan synthase
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1,4-beta-glucan synthase
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beta-1,4-glucan synthase
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beta-1,4-glucan synthetase
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beta-1,4-glucosyltransferase
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beta-glucan synthase
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cellulose syntethase
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cellulose synthase (UDP-forming)
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cellulose synthase (uridine diphosphate-forming)
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cellulose synthase 3
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cellulose synthase A
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cellulose synthase complex
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glucan synthase
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glucosyltransferase, uridine diphosphoglucose-1,4-beta-glucan
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GS-I
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UDP-glucose-1,4-beta-glucan glucosyltransferase
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UDP-glucose-dependent beta-1,4-glucan synthase
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UDP-glucose:1,4-beta-D-glucan 4-beta-D-glucosyltransferase
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UDPglucose-beta-glucan glucosyltransferase
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UDPglucose-cellulose glucosyltransferase
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uridine diphosphoglucose-cellulose glucosyltransferase
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additional information
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexosyl group transfer
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
UDP-glucose:(1->4)-beta-D-glucan 4-beta-D-glucosyltransferase
Involved in the synthesis of cellulose. A similar enzyme utilizes GDP-glucose [EC 2.4.1.29 cellulose synthase (GDP-forming)].
CAS REGISTRY NUMBER
COMMENTARY hide
9027-19-4
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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 + [(1->4)-beta-D-glucosyl]n
UDP + [(1->4)-beta-D-glucosyl]n+1
show the reaction diagram
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?
UDP-alpha-D-glucose + [(1->4)-beta-D-glucosyl]n
UDP + [(1->4)-beta-D-glucosyl]n+1
show the reaction diagram
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?
additional information
?
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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 + [(1->4)-beta-D-glucosyl]n
UDP + [(1->4)-beta-D-glucosyl]n+1
show the reaction diagram
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?
UDP-alpha-D-glucose + [(1->4)-beta-D-glucosyl]n
UDP + [(1->4)-beta-D-glucosyl]n+1
show the reaction diagram
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?
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
1 mM used in assay conditions
Mn2+
1 mM used in assay conditions
Mg2+
1 mM used in assay conditions
Mn2+
1 mM used in assay conditions
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
isoxaben
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reduces cellulose synthesis in wild-type but not ixr1-1 seedlings
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
CESA3 and CESA6 are undetectable in imbibed seeds and appear after germination
Manually annotated by BRENDA team
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long, cylindrical cells, movement of the cellulose synthase complexes beneath the nascent secondary wall in developing xylem vessels, quantitative analysis, overview
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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the cellulose synthase-containing compartment moves rapidly beneath sites of secondary wall synthesis, overview
Manually annotated by BRENDA team
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cortical, the cellulose synthase-containing compartment moves rapidly beneath sites of secondary wall synthesis, overview
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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the naturally occuring irx3-1 and irx5-2 mutations are caused by premature stop codons that result in protein truncation of CESA7 and CESA4,respectively. In the naturally occuring irx3-1 background, interaction between CESA4 and CESA8 is greatly reduced, and the proteins fail to localize to the plasma membrane
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CESA6_ARATH
1084
8
122502
Swiss-Prot
other Location (Reliability: 5)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 130000, His6-tagged enzyme, SDS-PAGE
?
x * 130000, His6-tagged enzyme, SDS-PAGE
homodimer
isozyme CESA4
monomer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
AtCesA7 is phosphorylated in vivo at two serine residues in a region of hyper-variability between the cellulose synthase catalytic subunits. Full length endogenous CesA7 is degraded via a proteasome dependant pathway in whole plant extracts. Phosphorylation of the catalytic subunits may target them for degradation via a proteasome dependant pathway. This is a possible mechanism by which plants regulate the relative levels of the three proteins whose specific interaction are required to form an active cellulose synthase complex
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C37A
site-directed mutagenesis of the RING-motif leading to slightly decreased interaction with other CESA proteins, overview
C37A/C56A
site-directed mutagenesis of the RING-motif leading to decreased interaction with other CESA proteins, overview
C37A/C64A C37A/C79A
site-directed mutagenesis of the RING-motif leading to decreased interaction with other CESA proteins, overview
C56A
site-directed mutagenesis of the RING-motif leading to slightly decreased interaction with other CESA proteins, overview
C56A/C64A
site-directed mutagenesis of the RING-motif leading to decreased interaction with other CESA proteins, overview
C56A/C79A C64A/C79A
site-directed mutagenesis of the RING-motif leading to decreased interaction with other CESA proteins, overview
C64A
site-directed mutagenesis of the RING-motif leading to slightly decreased interaction with other CESA proteins, overview
C79A
site-directed mutagenesis of the RING-motif leading to slightly decreased interaction with other CESA proteins, overview
P578S
identification of thanatos, a semidominant mutant of Arabidopsis thaliana with impaired growth of seedlings due to a mutation in the catalytic domain of cellulose synthase 3, homozygous seedlings of than germinate and grow but do not survive, while heterozygous plants are dwarfed and display a radially swollen root phenotype, cellulose content is reduced by approximately one-fifth in heterozygous and by two-fifths in homozygous plants, overview. Gene dosage-dependent expression of the AtCesA3 mutant gene in wild-type Arabidopsis thaliana plants results in a than dominant-negative phenotype. The mutation alters the structure of the CESA3 catalytic domain
additional information
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the naturally occuring irx3-1 and irx5-2 mutations are caused by premature stop codons that result in protein truncation of CESA7 and CESA4, respectively. In the naturally occuring irx3-1 background, interaction between CESA4 and CESA8 is greatly reduced, and the proteins fail to localize to the plasma membrane. Cellulose contents of mutant lines irx5 and irx1 plants recombinantly expressing CESA8 and CESA4, irx5-2:STREP-CESA4 and irx1-1:STREPCESA8, are much lower than wild-type and as such are not fully functional. Recombinant mutant irx3-1 plants expressing STREP-CESA7 and His/FLAGCESA7 in a dual tag system have wild-type cellulose content and xylem phenotypes, overview. irx3-1:STREP-CESA7-irx3-1:His/FLAG-CESA7 crossed plants phenotype, overview
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
full length endogenous CesA7 is degraded via a proteasome dependant pathway in whole plant extracts. Phosphorylation of the catalytic subunits may target them for degradation via a proteasome dependant pathway. This is a possible mechanism by which plants regulate the relative levels of the three proteins whose specific interaction are required to form an active cellulose synthase complex
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-agarose column chromatography
IRX3 ist tightly bound to the cell wall and can only be released using very harsh conditions. Triton X-100 and NP40 are most effective. No effect: Triton X-114, Tween 80, Brij 35, Brij 58, CHAPS, octyl beta-glucoside, octyl beta-thioglucopyranoside
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native oligomers partially from microsomes as fragments of the cellulose synthase complex by dual epitope tagging of the CESA7 protein, selection for CESA multimers, overview. Recombinant His- and STREP-tagged CESA4, CESA7, and CESA8, as well as double mutant irx3-1:STREP-CESA7-irx3-1:His/FLAG-CESA7 from Arabidopsis thaliana irx1-1, irx3-1, and irx5-2 mutant plants by nickel and streptavidin affinity chromatography
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Ni-agarose column chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Saccharomyces cerevisiae strain InvSc1
CesA and Csl genes, detailed phylogenetic analysis, overview
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expressed in Saccharomyces cerevisiae strain InvSc1
expression of His- and STREP-tagged CESA4, CESA7, and CESA8 in Arabidopsis thaliana using the Agrobacterium tumefaciens transfection nethod in the mutant lines are irx1-1, irx3-1, and irx5-2
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gene cesA, genotyping, quantitative real-time PCR assays, overview
interaction analysis between membrane-bound cellulose synthases using the yeast two-hybrid expression system in strain NMY51, confirmed by in planta by bimolecular fluorescence complementation assay, overview
usage of the CesA enzyme family from Arabidopsis thaliana for construction of a phylogeny-based CesA nomenclature for the Populus CesA gene family, aligning it with the enzyme family from Arabidopsis thaliana, phylogenetic analysis, overview
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Taylor, N.G.; Gardiner, J.C.; Whiteman, R.; Turner, S.R.
Cellulose synthesis in the Arabidopsis secondary cell wall
Cellulose
11
329-338
2004
Arabidopsis thaliana
-
Manually annotated by BRENDA team
Cano-Delgado, A.; Penfield, S.; Smith, C.; Catley, M.; Bevan, M.
Reduced cellulose synthesis invokes lignification and defense responses in Arabidopsis thaliana
Plant J.
34
351-362
2003
Arabidopsis thaliana
Manually annotated by BRENDA team
Singh, S.K.; Fischer, U.; Singh, M.; Grebe, M.; Marchant, A.
Insight into the early steps of root hair formation revealed by the procuste1 cellulose synthase mutant of Arabidopsis thaliana
BMC Plant Biol.
8
57
2008
Arabidopsis thaliana (Q94JQ6), Arabidopsis thaliana
Manually annotated by BRENDA team
Taylor, N.G.
Identification of cellulose synthase AtCesA7 (IRX3) in vivo phosphorylation sites - a potential role in regulating protein degradation
Plant Mol. Biol.
64
161-171
2007
Arabidopsis thaliana (Q9SWW6), Arabidopsis thaliana
Manually annotated by BRENDA team
Paredez, A.R.; Persson, S.; Ehrhardt, D.W.; Somerville, C.R.
Genetic evidence that cellulose synthase activity influences microtubule cortical array organization
Plant Physiol.
147
1723-1734
2008
Arabidopsis thaliana
Manually annotated by BRENDA team
Desprez, T.; Juraniec, M.; Crowell, E.F.; Jouy, H.; Pochylova, Z.; Parcy, F.; Hoefte, H.; Gonneau, M.; Vernhettes, S.
Organization of cellulose synthase complexes involved in primary cell wall synthesis in Arabidopsis thaliana
Proc. Natl. Acad. Sci. USA
104
15572-15577
2007
Arabidopsis thaliana (Q941L0), Arabidopsis thaliana (Q94JQ6), Arabidopsis thaliana
Manually annotated by BRENDA team
Yin, Y.; Huang, J.; Xu, Y.
The cellulose synthase superfamily in fully sequenced plants and algae
BMC Plant Biol.
9
99-112
2009
Arabidopsis thaliana, Oryza sativa, Phaeodactylum tricornutum, Populus trichocarpa, Sorghum bicolor, Vitis vinifera, Selaginella moellendorffii
Manually annotated by BRENDA team
Timmers, J.; Vernhettes, S.; Desprez, T.; Vincken, J.; Visser, R.; Trindade, L.
Interactions between membrane-bound cellulose synthases involved in the synthesis of the secondary cell wall
FEBS Lett.
583
978-982
2009
Arabidopsis thaliana (Q84JA6), Arabidopsis thaliana (Q8LPK5), Arabidopsis thaliana (Q9SWW6)
Manually annotated by BRENDA team
Atanassov, I.; Pittman, J.; Turner, S.
Elucidating the mechanisms of assembly and subunit interaction of the cellulose synthase complex of Arabidopsis secondary cell walls
J. Biol. Chem.
284
3833-3841
2009
Arabidopsis thaliana
Manually annotated by BRENDA team
Sandhu, A.; Randhawa, G.; Dhugga, K.
Plant cell wall matrix polysaccharide biosynthesis
Mol. Plant
2
840-850
2009
Arabidopsis thaliana, Hordeum vulgare, Oryza sativa
Manually annotated by BRENDA team
Daras, G.; Rigas, S.; Penning, B.; Milioni, D.; McCann, M.C.; Carpita, N.C.; Fasseas, C.; Hatzopoulos, P.
The thanatos mutation in Arabidopsis thaliana cellulose synthase 3 (AtCesA3) has a dominant-negative effect on cellulose synthesis and plant growth
New Phytol.
184
114-126
2009
Arabidopsis thaliana (Q941L0), Arabidopsis thaliana
Manually annotated by BRENDA team
Wightman, R.; Marshall, R.; Turner, S.
A cellulose synthase-containing compartment moves rapidly beneath sites of secondary wall synthesis
Plant Cell Physiol.
50
584-594
2009
Arabidopsis thaliana
Manually annotated by BRENDA team
Kumar, M.; Thammannagowda, S.; Bulone, V.; Chiang, V.; Han, K.; Joshi, C.; Mansfield, S.; Mellerowicz, E.; Sundberg, B.; Teeri, T.; Ellis, B.
An update on the nomenclature for the cellulose synthase genes in Populus
Trends Plant Sci.
14
248-254
2009
Arabidopsis thaliana, Populus alba, Populus deltoides, Populus x canadensis, Populus nigra, Populus tremula, Populus tremula x Populus alba, Populus tremula x Populus tremuloides, Populus tremuloides, Populus trichocarpa, Populus trichocarpa x Populus deltoides, Populus euphratica, Populus x tomentiglandulosa, Populus simonii, Populus balsamifera
Manually annotated by BRENDA team
Yang, J.; Bak, G.; Burgin, T.; Barnes, W.J.; Mayes, H.B.; Pena, M.J.; Urbanowicz, B.R.; Nielsen, E.
Biochemical and genetic analysis identify CSLD3 as a beta-1,4-glucan synthase that functions during plant cell wall synthesis
Plant Cell
32
1749-1767
2020
Arabidopsis thaliana (Q94JQ6), Arabidopsis thaliana (Q9M9M4)
Manually annotated by BRENDA team