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2.4.1.255: protein O-GlcNAc transferase

This is an abbreviated version!
For detailed information about protein O-GlcNAc transferase, go to the full flat file.

Word Map on EC 2.4.1.255

Reaction

UDP-N-acetyl-alpha-D-glucosamine
+
[protein]-L-serine
=
UDP
 +
[protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-L-serine

Synonyms

beta-N-acetylglucosaminidase, EGF domain-specific O-GlcNAc transferase, EGF domain-specific O-linked N-acetylglucosamine transferase, EOGT, EOGT1, epidermal growth factor domain-specific O-GlcNAc transferase, glycosyltransferase OGT, Gtf1, GtfA, hOGT, HsOGT, human OGT, mammalian OGT, mOGT, More, N-acetylglucosamine transferase, N-acetylglucosamine-peptide N-acetylglucosaminyltransferase, N-acetylglucosaminyltransferase, ncOGT, nuclear cytoplasmic OGT, nucleocytoplasmic glycosyltransferase, nucleocytoplasmic OGT, O-GlcNAc protein, O-GlcNAc transferase, O-GlcNAc transferase OGT, O-GlcNAc-transferase, O-GlcNAcase, O-glycosylated protein p135, O-linked beta-N-acetylglucosamine transferase, O-linked beta-N-acetylglucosaminyltransferase, O-linked GlcNAc transferase, O-linked N-acetylglucosamine transferase, O-linked N-acetylglucosaminyltransferase, O-N-acetylglucosamine (O-GlcNAc) transferase, OGT, OGT p110, OGT protein, ogta, OGTase, OGTase protein, ogtb, p135, Protein SECRET AGENT, SEC, SECRET AGENT, sOGT, spindly, SPY, super sex combs, Sxc, Synpcc7942_0051, transferase OGT, UDP-GlcNAc: polypeptide O-N-acetylglucosaminyltransferase, UDP-GlcNAc:polypeptidyl transferase, UDP-N-acetylglucosaminyl transferase, uridine diphosphate-N-acetyl-D-glucosamine:polypeptidyltransferase, uridine diphospho-N-acetylglucosamine:polypeptide beta-N-acetylaminyltransferase, uridine diphospho-N-acetylglucosamine:polypeptide beta-N-acetylglucosaminyltransferase, XcOGT, XcOGT protein

ECTree

     2 Transferases
         2.4 Glycosyltransferases
             2.4.1 Hexosyltransferases
                2.4.1.255 protein O-GlcNAc transferase

Engineering

Engineering on EC 2.4.1.255 - protein O-GlcNAc transferase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
sec spy double mutant
double-mutant embryos aborted at various stages of development and no double-mutant seedlings are obtained. These results indicate that OGT activity is required during gametogenesis and embryogenesis with lethality occurring when parentally derived SEC, SPY, and/or O-GlcNAcylated proteins become limiting
sec-1
has a tDNA insertion within the exon encoding the ninth tetratricopeptide repeat, no obvious phenotype. Two SEC tDNA insertional mutants are identified and analyzed. sec mutant plants do not exhibit obvious phenotypes, sec and spy mutations have a synthetic lethal interaction
sec-2
contains an insertion within an intron adjacent to exons encoding the putative catalytic portion of the protein, no obvious phenotype. Two SEC tDNA insertional mutants are identified and analyzed. sec mutant plants do not exhibit obvious phenotypes, sec and spy mutations have a synthetic lethal interaction
spy-3
Columbia (Col-0) background, has a Gly-to-Ser substitution in the C-terminal region of the protein. The spy plants have defects in a number of processes, including gibberellin and cytokinin responses, flowering, circadian regulation, and light inhibition of hypocotyls elongation
H537A
5.6% of wild-type activity
H596F
3.0% of wild-type activity
K872M
mutation of a key catalytic lysine, crystallized in complex with the inhibitor/substrate analogue UDP-5S-GlcNAc. Inactive
C835A
the mutation has no effect compared with wild type enzyme
C836S
-
site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD II, 10% activity compared to wild type
C839S
-
site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD II, less than 1% activity compared to wild type
C911A
active site mutant
C917A
D368A
activity is identical to wild-type enzyme
D386A/D420A
activity is 190% compared to wild-type enzyme
D386A/D420A/D454A
activity is 170% compared to wild-type enzyme
D407A
-
significant inhibitory effect on OGT enzyme activity, site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD I
D4209A/D454A
activity is 80% compared to wild-type enzyme
D420A
activity is 130% compared to wild-type enzyme
D422A
-
site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD I, produces a 50-100% increase in activity
D431A
single-point mutation, peptide-binding mutant
D438A
-
significant inhibitory effect on OGT enzyme activity, site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD I
D454A
activity is 130% compared to wild-type enzyme
D488A
-
significant inhibitory effect on OGT enzyme activity, site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD I
D505A
-
significant inhibitory effect on OGT enzyme activity, site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD I
D549A
-
significant inhibitory effect on OGT enzyme activity, site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD I
D554A
-
significant inhibitory effect on OGT enzyme activity, site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD I
D925A
D925N
single-point mutation, UDP-GlcNAc-binding mutant
DELTAN-DELTAKEN-FoxM1
-
O-GlcNAcation required the N terminus
E482A
-
significant inhibitory effect on OGT enzyme activity, site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD I
E556A
-
significant inhibitory effect on OGT enzyme activity, site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD I
E568A
-
significant inhibitory effect on OGT enzyme activity, site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD I
F439A
-
significant inhibitory effect on OGT enzyme activity, site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD I
F460A
-
significant inhibitory effect on OGT enzyme activity, site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD I
F721A
-
site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD II, 10% activity compared to wild type
F752A
-
site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD II, 110% activity compared to wild type
F776A
-
site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD II, 10% activity compared to wild type
G402S
-
significant inhibitory effect on OGT enzyme activity, site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD I
G453S
-
significant inhibitory effect on OGT enzyme activity, site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD I
G472A
-
significant inhibitory effect on OGT enzyme activity, site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD I
G538S
-
significant inhibitory effect on OGT enzyme activity, site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD I
H498A
single-point mutation, peptide-binding mutant
H558A
-
active site mutant
H558D
-
active site mutant
H558E
-
active site mutant
H901Y
-
active site mutant
H920A
-
active site mutant, deleterious
hOGT (26-end)
-
mutant
K842A
K842M
single-point mutation, UDP-GlcNAc-binding mutant
K898A
L796A
-
site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD II, less than 1% activity compared to wild type
N458A
single-point mutation, peptide-binding mutant
ncOGT
-
long OGT isoform, nucleocytoplasmic OGT, microinjected into immature oocytes prior to progesterone incubation
Q839A
single-point mutation, UDP-GlcNAc-binding mutant
Q839E
-
active site mutant
Q839N
-
active site mutant, low specific activity
R637A
single-point mutation, peptide-binding mutant
S18A/H127A
OGlcNAcylation on the mutant enzyme sharply declines
S52A
O-GlcNAcylation on the mutant enzyme increases
S56A
O-GlcNAcylation on the mutant enzyme increases
sOGT
-
N-terminally truncated isoform, short OGT, microinjected into immature oocytes prior to progesterone incubation
T12A
O-GlcNAcylation on the mutant enzyme declines
T12A/H127A
OGlcNAcylation on the mutant enzyme sharply declines
T12G
sharply reduced O-GlcNAcylation of short-form O-GlcNAc transferase
T12L
sharply reduced O-GlcNAcylation of short-form O-GlcNAc transferase
T12Y
sharply reduced O-GlcNAcylation of short-form O-GlcNAc transferase
T560A
single-point mutation, UDP-GlcNAc-binding mutant
T914A
active site mutant
T921A
T922A
active site mutant
W536A
-
significant inhibitory effect on OGT enzyme activity, site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD I
W735A
-
site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD II, less than 1% activity compared to wild type
W748A
-
site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD II, less than 1% activity compared to wild type
W812A
-
site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD II, less than 1% activity compared to wild type
W878A
-
site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD II, less than 1% activity compared to wild type
Y387A
-
significant inhibitory effect on OGT enzyme activity, site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD I, mutation is not included for enzymatic analysis, because not sufficient amounts of protein could be produced
Y434A
-
site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD I
Y539A
-
significant inhibitory effect on OGT enzyme activity, site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD I
Y841A
N263Q/N354Q
a decrease in O-GlcNAc stoichiometry is observed in Notch1 co-expressed with an N263Q/N354Q variant compared with wild-type enzyme. The N263Q/N354Q variant exhibits altered subcellular distribution within the endoplasmic reticulum in HEK293T cells, indicating that N-glycosylation of EOGT is required for its localization in the endoplasmic reticulum at the cell periphery
DELTA2.5OGT
-
Baculovirus-produced recombinant, is partially active toward the OID protein substrate, but is fully active toward the CKII peptide substrate
DELTA5.5OGT
-
Baculovirus-produced recombinant
full-length OGT
-
Baculovirus-produced recombinant
G350D
mutation corresponds to G570D mutation in Arabidopsis thaliana, results in plants with altered hormone responses, does not rescue the settling phenotype of the OGT deletion strain
H280A
mutation in residue corresponding to His residue in the human enzyme predicted to be important in the transfer of GlcNAc to substrates, does not rescue the settling phenotype of the OGT deletion strain
K445A
mutation in residue corresponding to His residue in the human enzyme predicted to be important in the transfer of GlcNAc to substrates, does not rescue the settling phenotype of the OGT deletion strain
G350D
-
mutation corresponds to G570D mutation in Arabidopsis thaliana, results in plants with altered hormone responses, does not rescue the settling phenotype of the OGT deletion strain
-
H280A
-
mutation in residue corresponding to His residue in the human enzyme predicted to be important in the transfer of GlcNAc to substrates, does not rescue the settling phenotype of the OGT deletion strain
-
K445A
-
mutation in residue corresponding to His residue in the human enzyme predicted to be important in the transfer of GlcNAc to substrates, does not rescue the settling phenotype of the OGT deletion strain
-
additional information