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Information on EC 2.4.99.18 - dolichyl-diphosphooligosaccharide-protein glycotransferase and Organism(s) Archaeoglobus fulgidus and UniProt Accession O29918

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IUBMB Comments
Occurs in eukaryotes that form a glycoprotein by the transfer of a glucosyl-mannosyl-glucosamine polysaccharide to the side-chain of an L-asparagine residue in the sequence -Asn-Xaa-Ser- or -Asn-Xaa-Thr- (Xaa not Pro) in nascent polypeptide chains. The basic oligosaccharide is the tetradecasaccharide Glc3Man9GlcNAc2 (for diagram {polysacc/Dol14}). However, smaller oligosaccharides derived from it and oligosaccharides with additional monosaccharide units attached may be involved. See ref for a review of N-glycoproteins in eukaryotes. Man3GlcNAc2 seems to be common for all of the oligosaccharides involved with the terminal N-acetylglucosamine linked to the protein L-asparagine. Occurs on the cytosolic face of the endoplasmic reticulum. The dolichol involved normally has 14-21 isoprenoid units with two trans double-bonds at the omega end, and the rest of the double-bonds in cis form.
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Archaeoglobus fulgidus
UNIPROT: O29918
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The taxonomic range for the selected organisms is: Archaeoglobus fulgidus
The expected taxonomic range for this enzyme is: Eukaryota, Archaea, Bacteria
Synonyms
oligosaccharyltransferase, oligosaccharyl transferase, oligosaccharyltransferase complex, ost3p, wbp1p, ost6p, oligosaccharide transferase, swp1p, tbstt3a, tbstt3b, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
AglB
archaeal homolog to bacterial PglB and eukaryotic Stt3
oligosaccharyltransferase
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AglB
archaeal homolog to bacterial PglB and eukaryotic Stt3
asparagine N-glycosyltransferase
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dolichyldiphosphooligosaccharide-protein oligosaccharyltransferase
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glycosyltransferase, dolichyldiphosphooligosaccharide-protein
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glycosyltransferase, dolichylpyrophosphodiacetylchitobiose-protein
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oligomannosyltransferase
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oligosaccharide transferase
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oligosaccharyltransferase
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oligosaccharyltransferase, dolichyldiphosphoryloligosaccharide-protein
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OST
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexosyl group transfer
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SYSTEMATIC NAME
IUBMB Comments
dolichyl-diphosphooligosaccharide:protein-L-asparagine N-beta-D-oligopolysaccharidotransferase
Occurs in eukaryotes that form a glycoprotein by the transfer of a glucosyl-mannosyl-glucosamine polysaccharide to the side-chain of an L-asparagine residue in the sequence -Asn-Xaa-Ser- or -Asn-Xaa-Thr- (Xaa not Pro) in nascent polypeptide chains. The basic oligosaccharide is the tetradecasaccharide Glc3Man9GlcNAc2 (for diagram {polysacc/Dol14}). However, smaller oligosaccharides derived from it and oligosaccharides with additional monosaccharide units attached may be involved. See ref [2] for a review of N-glycoproteins in eukaryotes. Man3GlcNAc2 seems to be common for all of the oligosaccharides involved with the terminal N-acetylglucosamine linked to the protein L-asparagine. Occurs on the cytosolic face of the endoplasmic reticulum. The dolichol involved normally has 14-21 isoprenoid units with two trans double-bonds at the omega end, and the rest of the double-bonds in cis form.
CAS REGISTRY NUMBER
COMMENTARY hide
75302-32-8
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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
dolichyl diphosphooligosaccharide + [protein]-L-asparagine
dolichyl diphosphate + [protein]-L-asparagine-N-oligosaccharide
show the reaction diagram
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a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine
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?
dolichyl diphosphooligosaccharide + [protein]-L-asparagine
dolichyl diphosphate + [protein]-L-asparagine-oligosaccharide
show the reaction diagram
i.e. substrate peptide LLO prepared from Pyrococcus furiosus cells and a substrate peptide, TAMRAAla-Pro-Tyr-Asn-Val-Thr-Lys-Arg, which is optimized by peptide library experiments
a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine, product analysis by mass spectrometry
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?
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
dolichyl diphosphooligosaccharide + [protein]-L-asparagine
dolichyl diphosphate + [protein]-L-asparagine-N-oligosaccharide
show the reaction diagram
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a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine
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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
the catalytic subunit of OST is called STT3 in eukaryotes, AglB in archaea, and PglB in eubacteria. Archaeoglobus f ulgidus encodes three AglB paralogues, two of them are the shortest AglBs across all domains of life.
physiological function
oligosaccharyltransferase transfers glycan to asparagine in the N-glycosylation sequon, the lysine and isoleucine residues in the DK/MI motif participate in the Ser/Thr recognition in the sequon
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
C-terminal globular domain of the of the smallest AglB, purified recombinant wild-type and selenomethionine-labeled AgBs, sitting and hanging drop vapor diffusion methods, crystals grow from a hanging drop with a 1:1 volume ratio of the protein stock solution containing 20 mg/mL protein in 20 mM Tris buffer, pH 8.0, and the reservoir solution containing 0.1 M MES buffer, pH 6.5, and 12.5% PEG 3350, at 20°C, soaking of crystals in reservoir solution with 20% ethylene glycol added for cryoprotection, X-ray diffraction structure determination and analysis at 1.75-1.94 A resolution
sitting drop vapor diffusion method, crystal structure of the C-terminal globular domain of the AglB paralog, AglB-Long, at 1.9 A resolutions
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D520A
site-directed mutagensis of the AglB-S1 subunit of OST, the mutant cannot be expressed in Escherichia coli
D520N
site-directed mutagensis of the AglB-S1 subunit of OST, the mutant shows reduced OST activity compared to the wild-type enzyme
D526A
site-directed mutagensis of the AglB-S1 subunit of OST, the mutant cannot be expressed in Escherichia coli
E521A
site-directed mutagensis of the AglB-S1 subunit of OST, the mutant cannot be expressed in Escherichia coli
E521Q
site-directed mutagensis of the AglB-S1 subunit of OST, the mutant shows reduced OST activity compared to the wild-type enzyme
I522A
site-directed mutagensis of the AglB-S1 subunit of OST, the mutant shows reduced OST activity compared to the wild-type enzyme
I535A
site-directed mutagensis of the AglB-S1 subunit of OST, the mutant cannot be expressed in Escherichia coli
K531A
site-directed mutagensis of the AglB-S1 subunit of OST, the mutant shows similar OST activity compared to the wild-type enzyme
K531D
site-directed mutagensis of the AglB-S1 subunit of OST, the mutant shows reduced OST activity compared to the wild-type enzyme
K531E
site-directed mutagensis of the AglB-S1 subunit of OST, the mutant shows reduced OST activity compared to the wild-type enzyme
K531R
site-directed mutagensis of the AglB-S1 subunit of OST, the mutant shows reduced OST activity compared to the wild-type enzyme
M524A
site-directed mutagensis of the AglB-S1 subunit of OST, the mutant cannot be expressed in Escherichia coli
N528A
site-directed mutagensis of the AglB-S1 subunit of OST, the mutant shows reduced OST activity compared to the wild-type enzyme
T518A
site-directed mutagensis of the AglB-S1 subunit of OST, the mutant cannot be expressed in Escherichia coli
T523A
site-directed mutagensis of the AglB-S1 subunit of OST, the mutant shows reduced OST activity compared to the wild-type enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant N-terminally His6-tagged wild-type and selenomethionine-labeled AglB from Escherichia coli strain BL21 by nickel affinity chromatography and gel filtration, followed by anion exchange chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloning of DNA encoding the full-length AfAglB-S1 gene, expression of N-terminally His6-tagged wild-type and selenomethionine-labeled AglB in Escherichia coli strains BL21(DE3) and C43(DE3), respectively
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Magidovich, H.; Eichler, J.
Glycosyltransferases and oligosaccharyltransferases in Archaea: putative components of the N-glycosylation pathway in the third domain of life
FEMS Microbiol. Lett.
300
122-130
2009
Archaeoglobus fulgidus (O29867), Archaeoglobus fulgidus (O29918), Archaeoglobus fulgidus (O30195), Caldivirga maquilingensis (A8MBU0), Candidatus Korarchaeum cryptofilum (B1L5S3), Desulfurococcus amylolyticus (B8D352), Haloarcula marismortui (Q5V4T7), Halobacterium salinarum (B0R4T2), Halobacterium salinarum NRC-1 (Q9HQP2), Haloquadratum walsbyi (Q18GV3), Halorubrum lacusprofundi (B9LMS1), Hyperthermus butylicus (A2BM28), Ignicoccus hospitalis (A8A8E8), Metallosphaera sedula (A4YHQ7), Methanobrevibacter smithii (A5UL43), Methanocaldococcus jannaschii (Q58920), Methanocella arvoryzae MRE50 (Q0W803), Methanocella arvoryzae MRE50 (Q0W817), Methanocella arvoryzae MRE50 (Q0W818), Methanococcoides burtonii (Q12VP3), Methanococcus aeolicus (A6UWW3), Methanococcus maripaludis C5 (A4FWA0), Methanococcus maripaludis C6 (A9A9N9), Methanococcus maripaludis C7 (A6VH10), Methanococcus maripaludis S2 (Q6LXC8), Methanococcus vannielii (A6UQ69), Methanocorpusculum labreanum (A2SR78), Methanoculleus marisnigri (A3CRV9), Methanoculleus marisnigri (A3CXQ8), Methanoregula boonei (A7I4W0), Methanoregula boonei (A7I7L6), Methanosarcina acetivorans (Q8TJM6), Methanosarcina acetivorans (Q8TJM7), Methanosarcina acetivorans (Q8TJM8), Methanosarcina acetivorans (Q8TRK3), Methanosarcina barkeri (Q46FJ0), Methanosarcina barkeri (Q46FW5), Methanosarcina barkeri (Q46FW6), Methanosarcina mazei (Q8PUW8), Methanosarcina mazei (Q8PZ47), Methanosarcina mazei (Q8PZ48), Methanosphaera stadtmanae (Q2NHD2), Methanosphaerula palustris (B8GG73), Methanospirillum hungatei (Q2FSJ2), Methanospirillum hungatei (Q2FTM5), Methanospirillum hungatei (Q2FUP2), Methanothermobacter thermautotrophicus str. Delta H (O27660), Methanothrix thermoacetophila (A0B8C2), Methanothrix thermoacetophila (A0B996), Nanoarchaeum equitans (Q74MN3), Natronomonas pharaonis (Q3IPK0), Nitrosopumilus maritimus (A9A114), no activity in Aeropyrum pernix, no activity in Methanopyrus kandleri, Picrophilus torridus (Q6L0Y1), Pyrobaculum aerophilum (Q8ZTY7), Pyrobaculum arsenaticum (A4WLR5), Pyrobaculum calidifontis (A3MUV5), Pyrobaculum islandicum (A1RRM7), Pyrobaculum neutrophilum (B1YAG2), Pyrococcus abyssi (Q9UYP5), Pyrococcus abyssi (Q9UZF5), Pyrococcus abyssi (Q9V250), Pyrococcus furiosus (Q8U3P6), Pyrococcus furiosus (Q8U4D2), Pyrococcus horikoshii (O58981), Pyrococcus horikoshii (O74088), Saccharolobus solfataricus (Q97Z77), Staphylothermus marinus (A3DL26), Sulfolobus acidocaldarius (Q4J9B4), Sulfurisphaera tokodaii (Q973G2), Thermococcus kodakarensis (Q5JH70), Thermococcus kodakarensis (Q5JJ26), Thermococcus onnurineus (B6YVI6), Thermococcus onnurineus (B6YVU0), Thermofilum pendens (A1RXW3), Thermoplasma acidophilum (Q9HJ37), Thermoplasma volcanium (Q979C6)
Manually annotated by BRENDA team
Matsumoto, S.; Igura, M.; Nyirenda, J.; Matsumoto, M.; Yuzawa, S.; Noda, N.; Inagaki, F.; Kohda, D.
Crystal structure of the C-terminal globular domain of oligosaccharyltransferase from Archaeoglobus fulgidus at 1.75 A resolution
Biochemistry
51
4157-4166
2012
Archaeoglobus fulgidus (O29918), Archaeoglobus fulgidus, Archaeoglobus fulgidus DSM 4306 (O29918)
Manually annotated by BRENDA team
Matsumoto, S.; Shimada, A.; Kohda, D.
Crystal structure of the C-terminal globular domain of the third paralog of the Archaeoglobus fulgidus oligosaccharyltransferases
BMC Struct. Biol.
13
11
2013
Archaeoglobus fulgidus (O29867), Archaeoglobus fulgidus
Manually annotated by BRENDA team