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Information on EC 2.4.1.133 - xylosylprotein 4-beta-galactosyltransferase and Organism(s) Drosophila melanogaster and UniProt Accession Q8T3P3
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2.4.1.133 xylosylprotein 4-beta-galactosyltransferaseIUBMB Comments
Involved in the biosynthesis of the linkage region of glycosaminoglycan chains as part of proteoglycan biosynthesis (chondroitin, dermatan and heparan sulfates). Requires Mn2+.
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Word Map
- 2.4.1.133
- proteoglycans
- glycosaminoglycans
- ehlers-danlos
- beta-1,4-galts
-
progeroid
-
xylosyltransferase
-
larsen
- hypermobility
- b3galt6
- laxity
-
hypermobl
-
reunion
-
linkeropathies
-
spondylodysplastic
-
hyperextensibility
- drug development
The taxonomic range for the selected organisms is: Drosophila melanogaster
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
galt i, b4galt7, galactosyltransferase i, beta-1,4-galt i, beta1,4-galt, beta-1,4-galt v, beta1,4-galt-i, galt-i, beta-1,4-galactosyltransferase i, beta4galt7, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
galactosyltransferase I
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-
-
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galactosyltransferase, uridine diphosphogalactose-xylose
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-
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proteoglycan UDP-galactose:beta-xylose beta 1,4-galactosyltransferase I
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UDP-D-galactose:D-xylose galactosyltransferase
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UDP-D-galactose:xylose galactosyltransferase
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-
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UDPgalactose:O-beta-D-xylosylprotein 4-beta-D-galactosyltransferase
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-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
UDP-alpha-D-galactose + [protein]-3-O-(beta-D-xylosyl)-L-serine = UDP + [protein]-3-O-(beta-D-galactosyl-(1->4)-beta-D-xylosyl)-L-serine
catalytic mechanism, oveview
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
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-
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PATHWAY SOURCE
PATHWAYS
KEGG
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-
SYSTEMATIC NAME
IUBMB Comments
UDP-galactose:O-beta-D-xylosylprotein 4-beta-D-galactosyltransferase
Involved in the biosynthesis of the linkage region of glycosaminoglycan chains as part of proteoglycan biosynthesis (chondroitin, dermatan and heparan sulfates). Requires Mn2+.
CAS REGISTRY NUMBER
COMMENTARY
52227-72-2
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UDP-galactose + O-beta-D-xylosylprotein
UDP + 4-beta-D-galactosyl-O-beta-D-xylosylprotein
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-
-
?
UDP-alpha-D-galactose + O-beta-D-xylosyl-[protein]
UDP + 4-beta-D-galactosyl-O-beta-D-xylosyl-[protein]
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-
-
?
UDP-galactose + O-beta-D-xylosylprotein
UDP + 4-beta-D-galactosyl-O-beta-D-xylosylprotein
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the enzyme transfers a galactose to the beta-xylose residue in proteolycan
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-
?
UDPgalactose + O-beta-D-xylosylprotein
UDP + 4-beta-D-galactosyl-O-beta-D-xylosylprotein
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the enzyme transfers a galactose to the beta-xylose residue in proteolycan. The enzyme is essential for viability
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-
?
UDPgalactose + p-nitrophenyl beta-D-xylopyranoside
UDP + beta-D-galactopyranosyl-1,4-xylopyranosyl-1-O-nitrophenol
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-
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?
UDPgalactose + p-nitrophenyl beta-D-xylose
UDP + beta-D-galactosyl-1,4-beta-D-xylosyl-1-O-nitrophenol
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-
-
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?
UDPgalactose + p-nitrophenyl N-acetyl-beta-D-glucosaminide
UDP + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminide-1-O-nitrophenol
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?
additional information
?
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donor and acceptor substrate binding, structure analysis, overview
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?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UDP-alpha-D-galactose + O-beta-D-xylosyl-[protein]
UDP + 4-beta-D-galactosyl-O-beta-D-xylosyl-[protein]
-
-
-
?
UDPgalactose + O-beta-D-xylosylprotein
UDP + 4-beta-D-galactosyl-O-beta-D-xylosylprotein
-
the enzyme transfers a galactose to the beta-xylose residue in proteolycan. The enzyme is essential for viability
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
the Drosophila enzyme exhibits only very low catalytic activity with magnesium
Mn2+
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
the enzyme is involved in proteoglycan synthesis
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme in the presence of manganese and UDP, hanging drop vapor diffusion method, using 100 mM Tris-HCl (pH 8.0), 1 M NaCl, 15% (v/v) MPD, and 5% (w/v) polyethylene glycol 6000
hanging drop vapor diffusion method, using 100 mM imidazole (pH 6.5) and 750 mM sodium acetate or 100 mM HEPES buffer (pH 8.0), 100mM serinol, 1.0 M NaCl, 5% (w/v) PEG6000, and 10% 2,4-methanepentadiol
purified recombinant detagged enzyme in complex xylobiose, hanging drop vapor diffusion method, mixing of protein solution containing 10 mg/ml protein, 10 mM MnCl2, 10 mM UDP, and 10 mM xylobiose, with a reservoir solution containing 100mM HEPES, pH 8.0, 100mM serinol, 1.0 M NaCl, 5% PEG 6000, and 10% 2-methyl-2,4-pentanediol, crystals of enzyme mutants D318N and D211N protein in complex with UDP-Gal, by hanging drop vapor diffusion method, using a protein solution containing 10 mg/ml protein, 10 mM MnCl2, and 10 mM UDP-Gal, with the precipitating solution containing 100 mM HEPES, pH 8.0, 1.0 M NaCl, 5% PEG 6000, and 10% 2-methyl-2,4-pentanediol, X-ray diffraction structure determination and analysis
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D211N
D211N
site-directed mutagenesis, the catalytic base Asp211 is mutated to Asn residue, inactive mutant, substrate-bound crystal structure analysis
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant N-terminally His6-tagged enzyme by affinity chromatography, and cleavage of the tag by TEV protease
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene B4GALT7, recombinant expression of N-terminally His6-tagged enzyme
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
100 mg of sulfonated protein are folded for 48 h in folding solution containing oxido-shuffling agents and 500 mM arginine-HCl
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Vadaie, N.; Hulinsky, R.S.; Jarvis, D.L.
Identification and characterization of a Drosophila melanogaster ortholog of human beta1,4-galactosyltransferase VII
Glycobiology
12
589-597
2002
Drosophila melanogaster
Bencurova, M.; Rendic, D.; Fabini, G.; Kopecky, E.M.; Altmann, F.; Wilson, I.B.H.
Expression of eukaryotic glycosyltransferases in the yeast Pichia pastoris
Biochimie
85
413-422
2003
Caenorhabditis elegans, Drosophila melanogaster
Takemae, H.; Ueda, R.; Okubo, R.; Nakato, H.; Izumi, S.; Saigo, K.; Nishihara, S.
Proteoglycan UDP-galactose:beta-xylose beta 1,4-galactosyltransferase I is essential for viability in Drosophila melanogaster
J. Biol. Chem.
278
15571-15578
2003
Drosophila melanogaster
Ramakrishnan, B.; Qasba, P.K.
Crystal structure of the catalytic domain of Drosophila beta1,4-Galactosyltransferase-7
J. Biol. Chem.
285
15619-15626
2010
Drosophila melanogaster (Q8T3P3)
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