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Information on EC 2.4.1.186 - glycogenin glucosyltransferase and Organism(s) Caenorhabditis elegans

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EC Tree
     2 Transferases
         2.4 Glycosyltransferases
             2.4.1 Hexosyltransferases
                2.4.1.186 glycogenin glucosyltransferase
IUBMB Comments
The first reaction of this enzyme is to catalyse its own glucosylation, normally at Tyr-194 of the protein if this group is free. When Tyr-194 is replaced by Thr or Phe, the enzyme's Mn2+-dependent self-glucosylation activity is lost but its intermolecular transglucosylation ability remains . It continues to glucosylate an existing glucosyl group until a length of about 5--13 residues has been formed. Further lengthening of the glycogen chain is then carried out by EC 2.4.1.11, glycogen (starch) synthase. The enzyme is not highly specific for the donor, using UDP-xylose in addition to UDP-glucose (although not glucosylating or xylosylating a xylosyl group so added). It can also use CDP-glucose and TDP-glucose, but not ADP-glucose or GDP-glucose. Similarly it is not highly specific for the acceptor, using water (i.e. hydrolysing UDP-glucose) among others. Various forms of the enzyme exist, and different forms predominate in different organs. Thus primate liver contains glycogenin-2, of molecular mass 66 kDa, whereas the more widespread form is glycogenin-1, with a molecular mass of 38 kDa.
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Caenorhabditis elegans
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The taxonomic range for the selected organisms is: Caenorhabditis elegans
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
glycogenin, glycogenin-1, glycogenin-2, priming glucosyltransferase, glycogenin 1, glycogenin 2, m-glycogenin, glycogenin glucosyltransferase, udp-glucose protein transglucosylase, proglycogen synthase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glucosyltransferase, uridine diphosphoglucose-protein
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glucosyltransferase, uridine diphosphoglucose-protein 4-alpha-
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glycogen initiator synthase
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glyogenin
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priming glucosyltransferase
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proglycogen synthase
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UDP-glucose protein transglucosylase
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UDP-glucose-protein glucosyltransferase
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UDP-glucose:protein glucosyltransferase
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UDPGlc:protein transglucosylase
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UPTG
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uridine diphosphate glucose-protein transglucosylase I
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uridine diphosphoglucose protein transglucosylase I
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uridine diphosphoglucose-protein 4-alpha-glucosyltransferase
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uridine diphosphoglucose-protein glucosyltransferase
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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-alpha-D-glucose:glycogenin alpha-D-glucosyltransferase
The first reaction of this enzyme is to catalyse its own glucosylation, normally at Tyr-194 of the protein if this group is free. When Tyr-194 is replaced by Thr or Phe, the enzyme's Mn2+-dependent self-glucosylation activity is lost but its intermolecular transglucosylation ability remains [7]. It continues to glucosylate an existing glucosyl group until a length of about 5--13 residues has been formed. Further lengthening of the glycogen chain is then carried out by EC 2.4.1.11, glycogen (starch) synthase. The enzyme is not highly specific for the donor, using UDP-xylose in addition to UDP-glucose (although not glucosylating or xylosylating a xylosyl group so added). It can also use CDP-glucose and TDP-glucose, but not ADP-glucose or GDP-glucose. Similarly it is not highly specific for the acceptor, using water (i.e. hydrolysing UDP-glucose) among others. Various forms of the enzyme exist, and different forms predominate in different organs. Thus primate liver contains glycogenin-2, of molecular mass 66 kDa, whereas the more widespread form is glycogenin-1, with a molecular mass of 38 kDa.
CAS REGISTRY NUMBER
COMMENTARY hide
117590-73-5
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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 + glycogenin
UDP + alpha-D-glucosylglycogenin
show the reaction diagram
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self-glucosylation of the glycosyltransferase glycogenin
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?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
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glycogenin is a member of the GT8 family of glycosyltransferases with a GT-A architecture
additional information
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interaction and binding of wild-type full-length enzyme and truncated mutant CeGN34 to glycogen synthase, the CeGS-CeGN34 interaction is required for glycogen formation, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
GYG1_CAEEL
429
0
49007
Swiss-Prot
other Location (Reliability: 3)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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glycogenin is a member of the GT8 family of glycosyltransferases with a GT-A architecture containing an N-terminal catalytic domain with a single Rossmann fold that operates as an obligate dimer. The core catalytic domain is followed by a C-terminal extension of variable length and undefined structure. Oligomerization of glycogenin and glycogen synthase from Caenorhabditis elegans enhances binding through an avidity effect
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
glycogen synthase-glycogenin enzyme complex, PDB ID 4QLB, GS-N interaction surface, overview
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Y194F
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site-directed mutagenesis, inactive mutant
additional information
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construction of a truncated enzyme version CeGN34. The CeGNDELTAC mutant is defective for interaction with glycogen synthase CeGS
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Zeqiraj, E.; Tang, X.; Hunter, R.; Garcia-Rocha, M.; Judd, A.; Deak, M.; Von Wilamowitz-Moellendorff, A.; Kurinov, I.; Guinovart, J.; Tyers, M.; Sakamoto, K.; Sicheri, F.
Structural basis for the recruitment of glycogen synthase by glycogenin
Proc. Natl. Acad. Sci. USA
111
E2831-E2840
2014
Caenorhabditis elegans
Manually annotated by BRENDA team