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Information on EC 2.4.1.109 - dolichyl-phosphate-mannose-protein mannosyltransferase and Organism(s) Schizosaccharomyces pombe and UniProt Accession O13898

for references in articles please use BRENDA:EC2.4.1.109
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IUBMB Comments
The enzyme transfers mannosyl residues to the hydroxy group of serine or threonine residues, producing cell-wall mannoproteins. It acts only on long-chain alpha-dihydropolyprenyl derivatives, larger than C35.
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Schizosaccharomyces pombe
UNIPROT: O13898
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The taxonomic range for the selected organisms is: Schizosaccharomyces pombe
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
pomt1, pomt2, protein o-mannosyltransferase, pmt1p, o-mannosyltransferase, protein o-mannosyltransferase 1, pmt2p, pmt1p-pmt2p, pmt4p, aapmta, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dolichyl-phosphate-mannose--protein mannosyltransferase 1
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O-glycoside mannosyltransferase
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dolichol phosphomannose-protein mannosyltransferase
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dolichyl-phosphate-mannose--protein mannosyltransferase 2
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dolichyl-phosphate-mannose--protein mannosyltransferase 4
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mannosyltransferase, dolichol phosphomannose-protein
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O-glycoside mannosyltransferase
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protein O-D-mannosyltransferase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexosyl group transfer
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SYSTEMATIC NAME
IUBMB Comments
dolichyl-phosphate-D-mannose:protein O-D-mannosyltransferase
The enzyme transfers mannosyl residues to the hydroxy group of serine or threonine residues, producing cell-wall mannoproteins. It acts only on long-chain alpha-dihydropolyprenyl derivatives, larger than C35.
CAS REGISTRY NUMBER
COMMENTARY hide
74315-99-4
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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 phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
O-glycosylation initiated by Ogm proteins plays crucial physiological roles and can serve as a sorting determinant for protein transport of membrane glycoproteins. While none of the ogm genes is found to be essential, ogm1D mutants differ morphologically from wildtype and exhibit defects in sexual agglutination. O-glycosylation of chitinase from Saccharomyces cerevisiae is decreased in ogm1D cells
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-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
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 phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
O-glycosylation initiated by Ogm proteins plays crucial physiological roles and can serve as a sorting determinant for protein transport of membrane glycoproteins. While none of the ogm genes is found to be essential, ogm1D mutants differ morphologically from wildtype and exhibit defects in sexual agglutination. O-glycosylation of chitinase from Saccharomyces cerevisiae is decreased in ogm1D cells
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-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Saccharomyces cerevisiae
expression in Saccharomyces cerevisiae
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tanaka, N.; Fujita, Y.; Suzuki, S.; Morishita, M.; Giga-Hama, Y.; Shimoda, C.; Takegawa, K.
Characterization of O-mannosyltransferase family in Schizosaccharomyces pombe
Biochem. Biophys. Res. Commun.
330
813-820
2005
Schizosaccharomyces pombe (O13898), Schizosaccharomyces pombe (O42933), Schizosaccharomyces pombe (Q9C100), Schizosaccharomyces pombe
Manually annotated by BRENDA team
Willer, T.; Brandl, M.; Sipiczki, M.; Strahl, S.
Protein O-mannosylation is crucial for cell wall integrity, septation and viability in fission yeast
Mol. Microbiol.
57
156-170
2005
Schizosaccharomyces pombe
Manually annotated by BRENDA team
Lengeler, K.B.; Tielker, D.; Ernst, J.F.
Protein-O-mannosyltransferases in virulence and development
Cell. Mol. Life Sci.
65
528-544
2008
Candida albicans (O74189), Candida albicans (Q59X23), Candida albicans (Q5ACU3), Candida albicans (Q5ADM9), Candida albicans (Q9UVB5), Cryptococcus neoformans, Mycobacterium tuberculosis, Saccharomyces cerevisiae (P31382), Saccharomyces cerevisiae (P33775), Saccharomyces cerevisiae (P42934), Saccharomyces cerevisiae (P46971), Saccharomyces cerevisiae (P47190), Saccharomyces cerevisiae (P52867), Saccharomyces cerevisiae (Q06644), Schizosaccharomyces pombe (O13898), Schizosaccharomyces pombe (O42933), Schizosaccharomyces pombe (Q9C100)
Manually annotated by BRENDA team