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Information on EC 2.4.1.153 - UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminyltransferase and Organism(s) Methanococcus voltae and UniProt Accession B3VA58

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IUBMB Comments
The enzyme, characterized from the methanogenic archaeon Methanococcus voltae, initiates N-linked glycosylation in that organism. The enzyme differs from the eukaryotic enzyme, which leaves one additional phosphate group on the dolichyl product (cf. EC 2.7.8.15, UDP-N-acetylglucosamine---dolichyl-phosphate N-acetylglucosaminephosphotransferase).
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Methanococcus voltae
UNIPROT: B3VA58
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The taxonomic range for the selected organisms is: Methanococcus voltae
The expected taxonomic range for this enzyme is: Eukaryota, Archaea
Synonyms
acetylglucosaminyltransferase, uridine diphosphoacetylglucosamine-dolichol phosphate, AglK, Dol-P-GlcNAc synthase, dolichyl phosphate acetylglucosaminyltransferase, dolichyl phosphate N-acetylglucosaminyltransferase, dolichyl-phosphate alpha-N-acetylglucosaminyltransferase, UDP-N-acetylglucosamine-dolichol phosphate N-acetylglucosaminyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Dol-P-GlcNAc synthase
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acetylglucosaminyltransferase, uridine diphosphoacetylglucosamine-dolichol phosphate
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dolichyl phosphate acetylglucosaminyltransferase
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dolichyl phosphate N-acetylglucosaminyltransferase
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dolichyl-phosphate alpha-N-acetylglucosaminyltransferase
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UDP-N-acetylglucosamine-dolichol phosphate N-acetylglucosaminyltransferase
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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-N-acetyl-D-glucosamine:dolichyl-phosphate alpha-N-acetyl-D-glucosaminyltransferase
The enzyme, characterized from the methanogenic archaeon Methanococcus voltae, initiates N-linked glycosylation in that organism. The enzyme differs from the eukaryotic enzyme, which leaves one additional phosphate group on the dolichyl product (cf. EC 2.7.8.15, UDP-N-acetylglucosamine---dolichyl-phosphate N-acetylglucosaminephosphotransferase).
CAS REGISTRY NUMBER
COMMENTARY hide
63363-73-5
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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-N-acetyl-alpha-D-glucosamine + dolichyl phosphate
UDP + dolichyl N-acetyl-alpha-D-glucosaminyl phosphate
show the reaction diagram
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-N-acetyl-alpha-D-glucosamine + dolichyl phosphate
UDP + dolichyl N-acetyl-alpha-D-glucosaminyl phosphate
show the reaction diagram
the enzyme initiates the N-linked glycan biosynthesis in the cytoplasm by transfer of N-acetyl-alpha-D-glucosamine to the membrane bound acceptor dolichyl phosphate
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-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
enzymatic activity requires divalent metal cations Ca2+, Mn2+, or Mg2+
Mg2+
enzymatic activity requires divalent metal cations Ca2+, Mn2+, or Mg2+
Mn2+
enzymatic activity requires divalent metal cations Ca2+, Mn2+, or Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
the enzyme initiates the N-linked glycan biosynthesis in the cytoplasm by transfer of N-acetyl-D-glucosamine to the membrane bound acceptor dolichyl phosphate. The recombinant enzyme produced in Escherichia coli sediments with the membrane fraction and requires detergent for solubility, suggesting it may contain hydrophobic regions that associate with the membrane
Manually annotated by BRENDA team
the enzyme initiates the N-linked glycan biosynthesis in the cytoplasm by transfer of N-acetyl-alpha-D-glucosamine to the membrane bound acceptor dolichyl phosphate. The recombinant enzyme produced in Escherichia coli sediments with the membrane fraction and requires detergent for solubility, suggesting it may contain hydrophobic regions that associate with the membrane
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
the enzyme initiates the N-linked glycan biosynthesis in the cytoplasm by transfer of N-acetyl-alpha-D-glucosamine to the membrane bound acceptor dolichyl phosphate
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
AGLK_METVO
251
0
28175
Swiss-Prot
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28175
x * 28175, calculated from sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 28175, calculated from sequence
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression in Escherichia coli with N-terminal T7 and C-terminal His6 tags
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Larkin, A.; Chang, M.M.; Whitworth, G.E.; Imperiali, B.
Biochemical evidence for an alternate pathway in N-linked glycoprotein biosynthesis
Nat. Chem. Biol.
9
367-373
2013
Methanococcus voltae (B3VA58), Methanococcus voltae PS (B3VA58)
Manually annotated by BRENDA team