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Information on EC 1.3.1.101 - 2,3-bis-O-geranylgeranyl-sn-glycerol 1-phosphate reductase [NAD(P)H] and Organism(s) Thermoplasma acidophilum and UniProt Accession Q9HKS9

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IUBMB Comments
A flavoprotein (FAD). The enzyme from the archaeon Thermoplasma acidophilum is involved in the biosynthesis of membrane lipids. In vivo the reaction occurs in the reverse direction with the formation of 2,3-bis-O-phytanyl-sn-glycerol 1-phosphate. cf. EC 1.3.7.11, 2,3-bis-O-geranylgeranyl-sn-glycero-phospholipid reductase.
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Thermoplasma acidophilum
UNIPROT: Q9HKS9
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The taxonomic range for the selected organisms is: Thermoplasma acidophilum
The expected taxonomic range for this enzyme is: Archaea, Bacteria
Synonyms
ta0516m, digeranylgeranylglycerophospholipid reductase, 2,3-digeranylgeranylglycerophospholipid reductase, dgggpl reductase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2,3-digeranylgeranylglycerophospholipid reductase
-
digeranylgeranylglycerophospholipid reductase
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SYSTEMATIC NAME
IUBMB Comments
2,3-bis-O-phytanyl-sn-glycerol 1-phosphate:NAD(P)+ oxidoreductase
A flavoprotein (FAD). The enzyme from the archaeon Thermoplasma acidophilum is involved in the biosynthesis of membrane lipids. In vivo the reaction occurs in the reverse direction with the formation of 2,3-bis-O-phytanyl-sn-glycerol 1-phosphate. cf. EC 1.3.7.11, 2,3-bis-O-geranylgeranyl-sn-glycero-phospholipid reductase.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2,3-bis-O-geranylgeranyl-sn-glycerol 1-phosphate + 8 NAD(P)H + 8 H+
2,3-bis-O-phytanyl-sn-glycerol 1-phosphate + 8 NAD(P)+
show the reaction diagram
2,3-bis-O-geranylgeranyl-sn-glyceryl 1-phosphate + 8 NAD(P)H + 8 H+
2,3-bis-O-phytanyl-sn-glycerol 1-phosphate + 8 NAD(P)+
show the reaction diagram
the enzyme catalyzes a critical step in the biosynthesis of archaeal membrane lipids. The saturation of hydrocarbon chains confers the ability to resist hydrolysis and oxidation and helps archaea withstand extreme conditions
-
-
?
2,3-bis-O-phytyl-sn-glycero-phosphoethanolamine + NAD(P)H + H+
?
show the reaction diagram
-
-
-
?
2,3-bis-O-phytyl-sn-glyceryl phosphate + NAD(P)H + H+
2,3-bis-O-phytanyl-sn-glycerol 1-phosphate + NAD(P)+
show the reaction diagram
-
-
-
?
3-O-(2,3-bis-O-phytyl-sn-glycero-phospho)-sn-glycerol + NAD(P)H + H+
?
show the reaction diagram
-
-
-
?
additional information
?
-
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
2,3-bis-O-geranylgeranyl-sn-glycerol 1-phosphate + 8 NAD(P)H + 8 H+
2,3-bis-O-phytanyl-sn-glycerol 1-phosphate + 8 NAD(P)+
show the reaction diagram
2,3-bis-O-geranylgeranyl-sn-glyceryl 1-phosphate + 8 NAD(P)H + 8 H+
2,3-bis-O-phytanyl-sn-glycerol 1-phosphate + 8 NAD(P)+
show the reaction diagram
the enzyme catalyzes a critical step in the biosynthesis of archaeal membrane lipids. The saturation of hydrocarbon chains confers the ability to resist hydrolysis and oxidation and helps archaea withstand extreme conditions
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD(P)H
required for activity
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0115
pH 6.5, 50°C, substrate: 2,3-di-O-geranylgeranyl-sn-glycerol 1-phosphate
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
membrane associated protein
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
the enzyme catalyzes a critical step in the biosynthesis of archaeal membrane lipids. The saturation of hydrocarbon chains confers the ability to resist hydrolysis and oxidation and helps archaea withstand extreme conditions
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43000
x * 43000, SDS-PAGE
45000
x * 45000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
vapor-diffusion method, crystal structure at 1.6 A resolution, in complex with flavin adenine dinucleotide (FAD) and a bacterial lipid
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli Rosetta (DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Xu, Q.; Eguchi, T.; Mathews, I.I.; Rife, C.L.; Chiu, H.J.; Farr, C.L.; Feuerhelm, J.; Jaroszewski, L.; Klock, H.E.; Knuth, M.W.; Miller, M.D.; Weekes, D.; Elsliger, M.A.; Deacon, A.M.; Godzik, A.; Lesley, S.A.; Wilson, I.A.
Insights into substrate specificity of geranylgeranyl reductases revealed by the structure of digeranylgeranylglycerophospholipid reductase, an essential enzyme in the biosynthesis of archaeal membrane lipids
J. Mol. Biol.
404
403-417
2010
Thermoplasma acidophilum (Q9HKS9), Thermoplasma acidophilum
Manually annotated by BRENDA team
Nishimura, Y.; Eguchi, T.
Stereochemistry of reduction in digeranylgeranylglycerophospholipid reductase involved in the biosynthesis of archaeal membrane lipids from Thermoplasma acidophilum
Bioorg. Chem.
35
276-283
2007
Thermoplasma acidophilum (Q9HKS9), Thermoplasma acidophilum
Manually annotated by BRENDA team
Nishimura, Y.; Eguchi, T.
Biosynthesis of archaeal membrane lipids: digeranylgeranylglycerophospholipid reductase of the thermoacidophilic archaeon Thermoplasma acidophilum
J. Biochem.
139
1073-1081
2006
Thermoplasma acidophilum (Q9HKS9), Thermoplasma acidophilum
Manually annotated by BRENDA team