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Information on EC 2.4.1.B58 - dolichol phosphate-mannose mannosyltransferase and Organism(s) Haloferax volcanii and UniProt Accession D4GYH0

for references in articles please use BRENDA:EC2.4.1.B58
preliminary BRENDA-supplied EC number
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EC Tree
     2 Transferases
         2.4 Glycosyltransferases
             2.4.1 Hexosyltransferases
                2.4.1.B58 dolichol phosphate-mannose mannosyltransferase
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Haloferax volcanii
UNIPROT: D4GYH0
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The taxonomic range for the selected organisms is: Haloferax volcanii
The expected taxonomic range for this enzyme is: Haloferax volcanii
Reaction Schemes
+
protein-bound glycan comprising the first four subunits of the N-linked pentasaccharide attached to the S-layer glycoprotein
=
+
protein-bound glycan comprising the N-linked pentasaccharide attached to the S-layer glycoprotein
Synonyms
hvo_1526, dolichol phosphate-mannose mannosyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
HVO_1526
locus name
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
dolichyl beta-D-mannosyl phosphate + protein-bound glycan comprising the first four subunits of the N-linked pentasaccharide attached to the S-layer glycoprotein
dolichyl phosphate + protein-bound glycan comprising the N-linked pentasaccharide attached to the S-layer glycoprotein
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
dolichyl beta-D-mannosyl phosphate + protein-bound glycan comprising the first four subunits of the N-linked pentasaccharide attached to the S-layer glycoprotein
dolichyl phosphate + protein-bound glycan comprising the N-linked pentasaccharide attached to the S-layer glycoprotein
show the reaction diagram
the enzyme is involved in the assembly a pentasaccharide to selected Asn residues of the S-layer glycoprotein in the archaeal N-glycosylation pathway
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
multispanning membrane protein
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
cells lacking HVO_1526 do not present peaks corresponding to the pentasaccharide-modified Asn-13-containing peptide. When cells of the deletion strain are transformed to express a polyhistidine-tagged version of HVO_1526, it is observed that the Asn-13-containing S-layer glycoprotein-derived peptide is once again modified by the complete pentasaccharide
physiological function
the enzyme is involved in the archaeal N-glycosylation pathway
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cohen-Rosenzweig, C.; Yurist-Doutsch, S.; Eichler, J.
AglS, a novel component of the Haloferax volcanii N-glycosylation pathway, is a dolichol phosphate-mannose mannosyltransferase
J. Bacteriol.
194
6909-6916
2012
Haloferax volcanii (D4GYH0), Haloferax volcanii, Haloferax volcanii DSM 3757 (D4GYH0)
Manually annotated by BRENDA team