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Information on EC 2.4.1.83 - dolichyl-phosphate beta-D-mannosyltransferase and Organism(s) Homo sapiens

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EC Tree
     2 Transferases
         2.4 Glycosyltransferases
             2.4.1 Hexosyltransferases
                2.4.1.83 dolichyl-phosphate beta-D-mannosyltransferase
IUBMB Comments
Acts only on long-chain polyprenyl phosphates and alpha-dihydropolyprenyl phosphates that are larger than C35.
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This record set is specific for:
Homo sapiens
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The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
dol-p-man synthase, dpm synthase, dolichol phosphate mannose synthase, mannosylphosphoryldolichol synthase, d-p-m, mpd synthase, dolichylphosphate mannose synthase, dolichyl-phosphate mannosyltransferase, mannosylphospho dolichol synthase, pfdpm1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Dol-P-Man-synthase
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Dol-P-Mansynthase
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dolichol phosphate mannose synthase
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dolichyl mannosyl phosphate synthase
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dolichyl phosphate mannosyltransferase
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dolichyl-phosphate mannose synthase
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dolichyl-phospho-mannose synthase
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DPMS
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GDP-Man:DolP mannosyltransferase
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GDP-mannose-dolichol phosphate mannosyltransferase
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GDPMan:DolP mannosyltransferase
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GDPmannose-dolichylmonophosphate mannosyltransferase
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GDPmannose:dolichyl-phosphate mannosyltransferase
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mannosylphosphodolichol synthase
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mannosylphosphoryldolichol synthase
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mannosyltransferase, guanosine diphosphomannose-dolichol phosphate
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MPD synthase
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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
GDP-mannose:dolichyl-phosphate beta-D-mannosyltransferase
Acts only on long-chain polyprenyl phosphates and alpha-dihydropolyprenyl phosphates that are larger than C35.
CAS REGISTRY NUMBER
COMMENTARY hide
62213-44-9
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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
GDPmannose + dolichyl phosphate
GDP + dolichyl D-mannosyl phosphate
show the reaction diagram
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
O60762; Q9P2X0
subunits Dpm1 and Dpm3 function as host dependency factors for Dengue virus and other related flaviviruses such as Zika virus. Mutation in the DXD motif of Dpm1, which is essential for its catalytic activity, abolishes DPMS-mediated Dengue virus infection. Genetic ablation of mannosyltransferase ALG3 renders cells poorly susceptible to Dengue virus. In cells deficient for DPMS activity, viral RNA amplification is hampered and truncated oligosaccharides are transferred to the viral precursor of the M protein and E glycoproteins, affecting their proper folding
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
DPM1_HUMAN
260
0
29634
Swiss-Prot
Mitochondrion (Reliability: 2)
Q5QPJ9_HUMAN
221
0
25106
TrEMBL
Mitochondrion (Reliability: 2)
Q5QPK2_HUMAN
287
0
32426
TrEMBL
Mitochondrion (Reliability: 2)
A0A804HJ93_HUMAN
132
0
15178
TrEMBL
other Location (Reliability: 1)
A0A804HIK9_HUMAN
188
0
21745
TrEMBL
Mitochondrion (Reliability: 2)
H0Y368_HUMAN
295
0
33350
TrEMBL
Mitochondrion (Reliability: 2)
A0A0S2Z4U1_HUMAN
133
0
15280
TrEMBL
Mitochondrion (Reliability: 2)
A0A804HIB3_HUMAN
129
0
14663
TrEMBL
Mitochondrion (Reliability: 2)
A0A0S2Z4Y5_HUMAN
260
0
29634
TrEMBL
Mitochondrion (Reliability: 2)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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enzyme consists of three subunits: DPM1, DPM2 and DPM3. DPM3 is stabilized by DPM2 and DPM3, in turn stabilizes the catalytic subunit DPM1
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene can complement a lethal null mutation in Schizosaccharomyces pombe
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
O60762; Q9P2X0
subunits Dpm1 and Dpm3 function as host dependency factors for Dengue virus and other related flaviviruses such as Zika virus. Mutation in the DXD motif of Dpm1, which is essential for its catalytic activity, abolishes DPMS-mediated Dengue virus infection. Genetic ablation of mannosyltransferase ALG3 renders cells poorly susceptible to Dengue virus. In cells deficient for DPMS activity, viral RNA amplification is hampered and truncated oligosaccharides are transferred to the viral precursor of the M protein and E glycoproteins, affecting their proper folding
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Colussi, P.A.; Taron, C.H.; Mack, J.C.; Orlean, P.
Human and Saccharomyces cerevisiae dolichol phosphate mannose synthases represent two classes of the enzyme, but both function in Schizosaccharomyces pombe
Proc. Natl. Acad. Sci. USA
94
7873-7878
1997
Homo sapiens (O60762), Homo sapiens, Saccharomyces cerevisiae
Manually annotated by BRENDA team
Maeda, Y.; Tanaka, S.; Hino, J.; Kangawa, K.; Kinoshita, T.
Human dolichol-phosphate-mannose synthase consists of three subunits, DPM1, DPM2 and DPM3
EMBO J.
19
2475-2482
2000
Homo sapiens
Manually annotated by BRENDA team
Labeau, A.; Simon-Loriere, E.; Hafirassou, M.L.; Bonnet-Madin, L.; Tessier, S.; Zamborlini, A.; Dupre, T.; Seta, N.; Schwartz, O.; Chaix, M.; Delaugerre, C.; Amara, A.; Meertens, L.
A genome-wide CRISPR-Cas9 screen identifies the dolichol-phosphate mannose synthase complex as a host dependency factor for dengue virus infection
J. Virol.
94
e01751
2020
Homo sapiens (O60762 and Q9P2X0)
Manually annotated by BRENDA team