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Information on EC 2.4.2.63 - EGF-domain serine xylosyltransferase and Organism(s) Homo sapiens and UniProt Accession Q8NBL1

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EC Tree
     2 Transferases
         2.4 Glycosyltransferases
             2.4.2 Pentosyltransferases
                2.4.2.63 EGF-domain serine xylosyltransferase
IUBMB Comments
The enzyme, found in animals and insects, xylosylates at the serine in the C-X-S-X-P-C motif of epidermal growth factor-like (EGF-like) domains. The enzyme is bifunctional also being active with UDP-alpha-glucose as donor (EC 2.4.1.376, EGF-domain serine glucosyltransferase).
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This record set is specific for:
Homo sapiens
UNIPROT: Q8NBL1
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Word Map
  • 2.4.2.63
  • artery
  • egypt
  • cairo
  • cardiac
  • ventricular
  • sham-operated
  • deficit
  • traumatic
  • egyptian
  • resuscitation
  • hemorrhage
  • injured
  • ischemia
  • infarct
  • hippocampus
  • trauma
  • occlusion
  • maze
  • depart
  • coronary
  • anesthetize
  • admitted
  • postoperative
  • reperfusion
  • systolic
  • post-injury
  • burn
  • echocardiography
  • ipsilateral
  • anesthesia
  • auditory
  • laparotomy
  • percussion
  • ringer
  • trauma-hemorrhage
  • hypoxia-ischemia
  • faculty
  • postburn
  • pressure-overloaded
  • time-matched
  • normothermia
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
+
[protein with EGF-like domain]-L-serine
=
+
[protein with EGF-like domain]-3-O-(beta-D-xylosyl)-L-serine
Synonyms
shams, glucoside xylosyltransferase, protein o-xylosyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
protein-O-glucosyltransferase 1
-
Poglut
-
-
Poxylt
-
-
protein O-xylosyltransferase
-
-
SYSTEMATIC NAME
IUBMB Comments
UDP-alpha-D-xylose:[protein with EGF-like domain]-L-serine O-beta-xylosyltransferase (configuration-inverting)
The enzyme, found in animals and insects, xylosylates at the serine in the C-X-S-X-P-C motif of epidermal growth factor-like (EGF-like) domains. The enzyme is bifunctional also being active with UDP-alpha-glucose as donor (EC 2.4.1.376, EGF-domain serine glucosyltransferase).
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-xylose + [factor VII protein with EGF-like domain 1]-L-serine
UDP + [factor VII protein with EGF-like domain 1]-3-O-(beta-D-xylosyl)-L-serine
show the reaction diagram
-
-
-
?
UDP-alpha-D-xylose + [Notch1 protein with EGF-like domain 12]-L-serine
UDP + [Notch1 protein with EGF-like domain 12]-3-O-(beta-D-xylosyl)-L-serine
show the reaction diagram
-
-
-
?
UDP-alpha-D-xylose + [factor VII protein with EGF-like domain]-L-serine
UDP + [factor VII protein with EGF-like domain]-3-O-(beta-D-xylosyl)-L-serine
show the reaction diagram
-
-
-
-
?
UDP-alpha-D-xylose + [Notch 2 protein with EGF-like domain]-L-serine
UDP + [Notch 2 protein with EGF-like domain]-3-O-(beta-D-xylosyl)-L-serine
show the reaction diagram
-
the di-serine motif within the O-glucose consensus sequence, CXSSPC, significantly enhances the enzyme activity
-
-
?
additional information
?
-
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-xylose + [factor VII protein with EGF-like domain 1]-L-serine
UDP + [factor VII protein with EGF-like domain 1]-3-O-(beta-D-xylosyl)-L-serine
show the reaction diagram
-
-
-
?
UDP-alpha-D-xylose + [Notch1 protein with EGF-like domain 12]-L-serine
UDP + [Notch1 protein with EGF-like domain 12]-3-O-(beta-D-xylosyl)-L-serine
show the reaction diagram
-
-
-
?
UDP-alpha-D-xylose + [factor VII protein with EGF-like domain]-L-serine
UDP + [factor VII protein with EGF-like domain]-3-O-(beta-D-xylosyl)-L-serine
show the reaction diagram
-
-
-
-
?
UDP-alpha-D-xylose + [Notch 2 protein with EGF-like domain]-L-serine
UDP + [Notch 2 protein with EGF-like domain]-3-O-(beta-D-xylosyl)-L-serine
show the reaction diagram
-
the di-serine motif within the O-glucose consensus sequence, CXSSPC, significantly enhances the enzyme activity
-
-
?
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
UDP-2-deoxy-2-fluoro-glucose
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PGLT1_HUMAN
392
0
46189
Swiss-Prot
Secretory Pathway (Reliability: 1)
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme in complexes with three different EGF-like domains and either UDP, UDP-2-deoxy-2-fluoro-glucose or UDP-methyl-glucose, hanging drop vapor diffusion method, using 10-20% (w/v) PEG 5000 MME, 50 mM MES pH 6.5, 2-10 mM CaCl2, 0-250 mM NaCl, 5-10% (v/v) glycerol or 2-methyl-2,4-pentanediol
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
IgG Sepharose affinity chromatography, HiTrap Sepharose column chromatography, and Superdex 200 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Drosophila melanogaster mutant clones
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Takeuchi, H.; Kantharia, J.; Sethi, M.; Bakker, H.; Haltiwanger, R.
Site-specific O-glucosylation of the epidermal growth factor-like (EGF) repeats of Notch Efficiency of glycosylation is affected by proper folding and amino acid sequence of individual EGF repeats
J. Biol. Chem.
287
33934-33944
2012
Homo sapiens
Manually annotated by BRENDA team
Li, Z.; Fischer, M.; Satkunarajah, M.; Zhou, D.; Withers, S.; Rini, J.
Structural basis of Notch O-glucosylation and O-xylosylation by mammalian protein-O-glucosyltransferase 1 (POGLUT1)
Nat. Commun.
8
185
2017
Homo sapiens (Q8NBL1)
Manually annotated by BRENDA team
Takeuchi, H.; Fernandez-Valdivia, R.; Caswell, D.; Nita-Lazar, A.; Rana, N.; Garner, T.; Weldeghiorghis, T.; Macnaughtan, M.; Jafar-Nejad, H.; Haltiwanger, R.
Rumi functions as both a protein O-glucosyltransferase and a protein O-xylosyltransferase
Proc. Natl. Acad. Sci. USA
108
16600-16605
2011
Homo sapiens, Mus musculus
Manually annotated by BRENDA team