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Information on EC 1.3.1.101 - 2,3-bis-O-geranylgeranyl-sn-glycerol 1-phosphate reductase [NAD(P)H]
for references in articles please use BRENDA:EC1.3.1.101
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EC Tree 1 Oxidoreductases
1.3 Acting on the CH-CH group of donors
1.3.1 With NAD+ or NADP+ as acceptor
1.3.1.101 2,3-bis-O-geranylgeranyl-sn-glycerol 1-phosphate reductase [NAD(P)H]
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.
The enzyme appears in viruses and cellular organisms
Reaction Schemes
showSynonyms
ta0516m, digeranylgeranylglycerophospholipid reductase, 2,3-digeranylgeranylglycerophospholipid reductase, dgggpl reductase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2,3-bis-(O-phytanyl)-sn-glycerol 1-phosphate + 8 NAD(P)+ = 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate + 8 NAD(P)H + 8 H+
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
archaetidylserine and archaetidylethanolamine biosynthesis
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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.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
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)+
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)+
Substrates: 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
Products: -
Products: -
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2,3-bis-O-phytyl-sn-glycero-phosphoethanolamine + NAD(P)H + H+
?
Substrates: -
Products: -
Products: -
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2,3-bis-O-phytyl-sn-glyceryl phosphate + NAD(P)H + H+
2,3-bis-O-phytanyl-sn-glycerol 1-phosphate + NAD(P)+
Substrates: -
Products: -
Products: -
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3-O-(2,3-bis-O-phytyl-sn-glycero-phospho)-sn-glycerol + NAD(P)H + H+
?
Substrates: -
Products: -
Products: -
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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)+
Substrates: formation of 2,3-di-O-phytanyl-sn-glyceryl phosphate (archaetidic acid), which is the basic core structure of archaeal membrane lipids
Products: -
Products: -
?
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)+
Substrates: formation of 2,3-di-O-phytanylglyceryl phosphate, which is the basic core structure of archaeal membrane lipids
Products: -
Products: -
?
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)+
Substrates: -
Products: -
Products: -
?
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)+
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: neither 2,3-bis-O-geranylgeranylglycerol nor 2,3-bis-O-geranylgeranylglyceryl phosphate dimethyl ester is recognized as a substrate
Products: -
Products: -
?
additional information
?
-
-
Substrates: neither 2,3-bis-O-geranylgeranylglycerol nor 2,3-bis-O-geranylgeranylglyceryl phosphate dimethyl ester is recognized as a substrate
Products: -
Products: -
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
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)+
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)+
Substrates: 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
Products: -
Products: -
?
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)+
Substrates: formation of 2,3-di-O-phytanyl-sn-glyceryl phosphate (archaetidic acid), which is the basic core structure of archaeal membrane lipids
Products: -
Products: -
?
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)+
Substrates: formation of 2,3-di-O-phytanylglyceryl phosphate, which is the basic core structure of archaeal membrane lipids
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
the sequence PxxYxWxFP defines a specificity pocket in the enzyme and precisely aligns the double bond of the geranyl group with respect to the FAD cofactor, thus providing a structural basis for the substrate specificity of geranylgeranyl reductases. FAD switches between two conformations that correspond to the reductive and oxidative half cycles. The structure provides evidence that substrate binding likely involves conformational changes, which are coupled to the two conformational states of the FAD
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
the enzyme does not require metal ions for activity
additional information
-
the enzyme does not require metal ions for activity
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0115
pH 6.5, 50°C, substrate: 2,3-di-O-geranylgeranyl-sn-glycerol 1-phosphate
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
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
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). GGR_PICTO
Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828 / KAW 2/3)
397
0
43748
Swiss-Prot
Mitochondrion (Reliability: 4)
GGR_THEVO
Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1)
396
0
43203
Swiss-Prot
Chloroplast (Reliability: 1)
GGR_THEAC
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
396
0
43353
Swiss-Prot
-
A0A0A7LEX9_9ARCH
396
0
43254
TrEMBL
-
A0A0Q0VQ29_9ARCH
397
0
43525
TrEMBL
Secretory Pathway (Reliability: 1)
A0A3G3IFM7_9ARCH
398
0
43194
TrEMBL
Chloroplast (Reliability: 5)
A0A8G2L7D4_PICTO
Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828 / KAW 2/3)
397
0
43748
TrEMBL
-
A0A8J7YJY6_9ARCH
395
0
43470
TrEMBL
-
A0A8J8CBS3_9ARCH
397
0
43058
TrEMBL
other Location (Reliability: 1)
A0A8J8PG77_9ARCH
391
0
42535
TrEMBL
-
A0A8J8TEJ8_9ARCH
396
0
42840
TrEMBL
-
M9SBC6_METAX
Methanomethylophilus alvi (strain Mx1201)
398
0
43194
TrEMBL
-
R9T7B0_METII
Methanomassiliicoccus intestinalis (strain Issoire-Mx1)
391
0
42487
TrEMBL
-
R9TB51_METII
Methanomassiliicoccus intestinalis (strain Issoire-Mx1)
396
0
42854
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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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
brenda
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
brenda
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
brenda
EXTERNAL LINKS (specific for EC-Number 1.3.1.101)
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