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Information on EC 2.4.1.259 - dolichyl-P-Man:Man6GlcNAc2-PP-dolichol alpha-1,2-mannosyltransferase and Organism(s) Arabidopsis thaliana and UniProt Accession Q9FZ49

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IUBMB Comments
The formation of N-glycosidic linkages of glycoproteins involves the ordered assembly of the common Glc3Man9GlcNAc2 core-oligosaccharide on the lipid carrier dolichyl diphosphate. Early mannosylation steps occur on the cytoplasmic side of the endoplasmic reticulum with GDP-Man as donor, the final reactions from Man5GlcNAc2-PP-Dol to Man9Glc-NAc2-PP-Dol on the lumenal side use dolichyl beta-D-mannosyl phosphate. ALG9 mannosyltransferase catalyses the addition of two different alpha-1,2-mannose residues - the addition of alpha-1,2-mannose to Man6GlcNAc2-PP-Dol (EC 2.4.1.259) and the addition of alpha-1,2-mannose to Man8GlcNAc2-PP-Dol (EC 2.4.1.261).
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Arabidopsis thaliana
UNIPROT: Q9FZ49
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The taxonomic range for the selected organisms is: Arabidopsis thaliana
The enzyme appears in selected viruses and cellular organisms
Synonyms
alg9 mannosyltransferase, dolichylphosphomannose-dependent alg9 mannosyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SYSTEMATIC NAME
IUBMB Comments
dolichyl beta-D-mannosyl phosphate:D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->3)-D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol alpha-1,2-mannosyltransferase
The formation of N-glycosidic linkages of glycoproteins involves the ordered assembly of the common Glc3Man9GlcNAc2 core-oligosaccharide on the lipid carrier dolichyl diphosphate. Early mannosylation steps occur on the cytoplasmic side of the endoplasmic reticulum with GDP-Man as donor, the final reactions from Man5GlcNAc2-PP-Dol to Man9Glc-NAc2-PP-Dol on the lumenal side use dolichyl beta-D-mannosyl phosphate. ALG9 mannosyltransferase catalyses the addition of two different alpha-1,2-mannose residues - the addition of alpha-1,2-mannose to Man6GlcNAc2-PP-Dol (EC 2.4.1.259) and the addition of alpha-1,2-mannose to Man8GlcNAc2-PP-Dol (EC 2.4.1.261).
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ALG9_ARATH
570
6
65083
Swiss-Prot
Mitochondrion (Reliability: 5)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
R100W
residue R100 is located near the end of the largest luminal loop between the first two predicted transmembrane segments and is absolutely conserved in all known ALG9 enzymes. Mutation suppresses a dwarf mutant, bri1-9, the phenotypes of which are caused by endoplasmic reticulum retention and endoplasmic reticulum-associated degradation of a brassinosteroid receptor, BRASSINOSTEROID-INSENSITIVE 1, BR1. The mutation prevents the Glc3Man9GlcNAc2 assembly and inhibits the endoplasmic reticulum-associated degradation of bri1-9. Overexpression of EBS4 in the R100W bri1-9 mutant, which encodes the Arabidopsis ortholog of the yeast ALG12 catalyzing the ER luminal alpha1,6 Man addition, adds an alpha1,6 Man to the truncated N-glycan precursor accumulated in R100W bri1-9, promotes the bri1-9 endoplasmic reticulum-associated degradation, and neutralizes the R100W suppressor phenotype
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hong, Z.; Kajiura, H.; Su, W.; Jin, H.; Kimura, A.; Fujiyama, K.; Li, J.
Evolutionarily conserved glycan signal to degrade aberrant brassinosteroid receptors in Arabidopsis
Proc. Natl. Acad. Sci. USA
109
11437-11442
2012
Arabidopsis thaliana (Q9FZ49)
Manually annotated by BRENDA team