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Information on EC 2.7.7.52 - RNA uridylyltransferase and Organism(s) Arabidopsis thaliana and UniProt Accession O64642

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EC Tree
     2 Transferases
         2.7 Transferring phosphorus-containing groups
             2.7.7 Nucleotidyltransferases
                2.7.7.52 RNA uridylyltransferase
IUBMB Comments
The enzyme requires an oligoribonucleotide or polyribonucleotide with a free terminal 3'-OH as a primer.
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This record set is specific for:
Arabidopsis thaliana
UNIPROT: O64642
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Word Map
  • 2.7.7.52
  • social
  • women
  • clinician
  • services
  • children
  • plan
  • physician
  • fabric
  • healthcare
  • perceived
  • professionals
  • decision
  • percept
  • demographic
  • film
  • user
  • theme
  • policy
  • psychological
  • skill
  • evidence-based
  • team
  • practitioner
  • surgeon
  • nanostructures
  • decision-making
  • emotional
  • psychosocial
  • thematic
  • tunable
  • semi-structured
  • nurses
  • rehabilitation
  • caregiver
  • satisfaction
  • dope
  • doping
  • stakeholder
  • semiconductor
  • self-management
  • optoelectronic
  • self-efficacy
  • sociodemographic
  • therapist
  • photoluminescence
  • violence
  • psycinfo
  • interpersonal
  • curriculum
  • self-care
  • medicine
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The enzyme appears in selected viruses and cellular organisms
Synonyms
tailor, tutase, zcchc11, terminal uridylyl transferase, heso1, rna editing tutase, terminal uridylyltransferase, meat1, tutase 1, u6-tutase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
terminal uridylyl transferase
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UTP: RNA uridylyltransferase
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UTP:RNA uridylyltransferase 1
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terminal uridylyltransferase
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-
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TUT
-
-
-
-
uridylyltransferase, terminal
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nucleotidyl group transfer
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
UTP:RNA uridylyltransferase
The enzyme requires an oligoribonucleotide or polyribonucleotide with a free terminal 3'-OH as a primer.
CAS REGISTRY NUMBER
COMMENTARY hide
78519-53-6
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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
UTP + miR158an
diphosphate + miR158an+1
show the reaction diagram
miR158a has the sequence 5'-Cy5-UCCCAAAUGUAGACAAAGCA-3'
-
-
?
UTP + miRNAn
diphosphate + miRNAn+1
show the reaction diagram
the enzyme URT1 plays a redundant but important role in miRNA uridylation when HESO1 is absent
-
-
?
UTP + mRNAn
diphosphate + mRNAn+1
show the reaction diagram
UTP + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
?
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
UTP + mRNAn
diphosphate + mRNAn+1
show the reaction diagram
for mRNA, URT1 is the main enzyme to uridylate the majority of mRNA and repairs their deadenylated ends to restore the binding site for poly(A) binding protein. Enzyme HESO1, on the other hand, targets mostly the mRNAs with very short oligo(A) tails and fails in fulfilling the same task
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-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
10 mM used in assay conditions
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
physiological function
isoform HESO1, which uridylates most unmethylated miRNAs in vivo, and isoform URT1 which exhibits nucleotidyl transferase activity on unmethylated miRNA, prefer substrates with different 3'-end nucleotides in vitro and act cooperatively to tail different forms of the same miRNAs in vivo. Both HESO1 and URT1 exhibit nucleotidyl transferase activity on AGO1-bound miRNAs. Although the enzymes are able to add long tails to AGO1-bound miRNAs, the tailed miRNAs remain associated with AGO1. Tailing of AGO1-bound miRNA165/6 drastically reduces the slicing activity of AGO1-miR165/6
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
URT1_ARATH
764
0
85764
Swiss-Prot
other Location (Reliability: 4)
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
mutant enzyme D547A, sitting drop vapor diffusion method, using 0.1 M HEPES, pH 7.5, 10% (w/v) PEG 6000 and 5% (w/v) 2-methyl-2,4-pentanediol
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D491A/D493A
complete loss of activity
D547A
catalytically dead mutant
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography and Superdex 200 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli Gold (DE3) cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sement, F.M.; Ferrier, E.; Zuber, H.; Merret, R.; Alioua, M.; Deragon, J.M.; Bousquet-Antonelli, C.; Lange, H.; Gagliardi, D.
Uridylation prevents 3 trimming of oligoadenylated mRNAs
Nucleic Acids Res.
41
7115-7127
2013
Arabidopsis thaliana (O64642), Arabidopsis thaliana Col-0 (O64642)
Manually annotated by BRENDA team
Tu, B.; Liu, L.; Xu, C.; Zhai, J.; Li, S.; Lopez, M.A.; Zhao, Y.; Yu, Y.; Ramachandran, V.; Ren, G.; Yu, B.; Li, S.; Meyers, B.C.; Mo, B.; Chen, X.
Distinct and cooperative activities of HESO1 and URT1 nucleotidyl transferases in microRNA turnover in Arabidopsis
PLoS Genet.
11
e1005119
2015
Arabidopsis thaliana (O64642), Arabidopsis thaliana (Q5XET5)
Manually annotated by BRENDA team
Zhu, L.; Hu, Q.; Cheng, L.; Jiang, Y.; Lv, M.; Liu, Y.; Li, F.; Shi, Y.; Gong, Q.
Crystal structure of Arabidopsis terminal uridylyl transferase URT1
Biochem. Biophys. Res. Commun.
524
490-496
2020
Arabidopsis thaliana (O64642)
Manually annotated by BRENDA team