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Information on EC 1.2.7.6 - glyceraldehyde-3-phosphate dehydrogenase (ferredoxin)
for references in articles please use BRENDA:EC1.2.7.6
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EC Tree 1 Oxidoreductases
1.2 Acting on the aldehyde or oxo group of donors
1.2.7 With an iron-sulfur protein as acceptor
1.2.7.6 glyceraldehyde-3-phosphate dehydrogenase (ferredoxin)
IUBMB Comments
Contains tungsten-molybdopterin and iron-sulfur clusters. This enzyme is thought to function in place of glyceralde-3-phosphate dehydrogenase and possibly phosphoglycerate kinase in the novel Embden-Meyerhof-type glycolytic pathway found in Pyrococcus furiosus . It is specific for glyceraldehyde-3-phosphate.
The expected taxonomic range for this enzyme is: Archaea, Bacteria
- 1.2.7.6
-
hyperthermophilic
- furiosus
- archaeon
-
embden-meyerhof
- tungsten
- formaldehyde
-
tungsten-containing
-
adp-dependent
- 3-phosphoglycerate
-
gluconeogenic
-
nonphosphorylating
- 6-phosphofructokinase
-
adp-forming
- glucokinase
-
ferredoxin-dependent
- pterin
-
volcanic
- aerophilum
- maripaludis
- degradation
-
methanococcus
- eucarya
-
pyrobaculum
-
tungstoenzymes
-
continental
-
phosphoglucose
- thermococcus
Reaction Schemes
showSynonyms
gapor, glyceraldehyde-3-phosphate ferredoxin oxidoreductase, glyceraldehyde-3-phosphate:ferredoxin oxidoreductase, gap:fdor, glyceraldehyde 3-phosphate ferredoxin oxidoreductase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
aldehyde ferredoxin oxidoreductase
dehydrogenase, glyceraldehyde phosphate (ferredoxin)
-
-
-
-
G3P:ferredoxin oxidoreductase
GAPOR
glyceraldehyde 3-phosphate oxidoreductase
glyceraldehyde phosphate dehydrogenase (ferredoxin)
-
-
-
-
glyceraldehyde-3-phosphate Fd oxidoreductase
-
-
-
-
glyceraldehyde-3-phosphate ferredoxin oxidoreductase
glyceraldehyde-3-phosphate ferredoxin reductase
-
-
-
-
glyceraldehyde-3-phosphate:ferredoxin oxidoreductase
Gor
PAE1029
GAPOR
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-glyceraldehyde-3-phosphate + H2O + oxidized ferredoxin = 3-phospho-D-glycerate + 2 H+ + reduced ferredoxin
D-glyceraldehyde-3-phosphate + H2O + oxidized ferredoxin = 3-phospho-D-glycerate + 2 H+ + reduced ferredoxin
this enzyme is thought to function in place of glyceraldehyde-3-phosphate dehydrogenase and possibly phosphoglycerate kinase in the novel Embden-Meyerhoff-type glycolytic pathway found in Pyrococcus furiosus. It is specific for glyceraldehyde-3-phosphate
-
D-glyceraldehyde-3-phosphate + H2O + oxidized ferredoxin = 3-phospho-D-glycerate + 2 H+ + reduced ferredoxin
this enzyme is thought to function in place of glyceraldehyde-3-phosphate dehydrogenase and possibly phosphoglycerate kinase in the novel Embden-Meyerhoff-type glycolytic pathway found in Pyrococcus furiosus. It is specific for glyceraldehyde-3-phosphate
D-glyceraldehyde-3-phosphate + H2O + oxidized ferredoxin = 3-phospho-D-glycerate + 2 H+ + reduced ferredoxin
electron transfer, mechanism and reduction potential
-
D-glyceraldehyde-3-phosphate + H2O + oxidized ferredoxin = 3-phospho-D-glycerate + 2 H+ + reduced ferredoxin
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
gluconeogenesis II (Methanobacterium thermoautotrophicum), glycolysis V (Pyrococcus)
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SYSTEMATIC NAME
IUBMB Comments
D-glyceraldehyde-3-phosphate:ferredoxin oxidoreductase
Contains tungsten-molybdopterin and iron-sulfur clusters. This enzyme is thought to function in place of glyceralde-3-phosphate dehydrogenase and possibly phosphoglycerate kinase in the novel Embden-Meyerhof-type glycolytic pathway found in Pyrococcus furiosus [1]. It is specific for glyceraldehyde-3-phosphate.
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CAS REGISTRY NUMBER
COMMENTARY
162995-20-2
-
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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
D-glyceraldehyde 3-phosphate + H2O + 2 oxidized benzyl viologen
3-phospho-D-glycerate + 2 H+ + 2 reduced benzyl viologen
Substrates: D-glyceraldehyde 3-phosphate is the only substrate oxidized by GAPOR, and the kinetics of the enzyme are unaffected by the presence of L-glyceraldehyde 3-phosphate
Products: -
Products: -
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D-glyceraldehyde 3-phosphate + H2O + 2 oxidized ferredoxin
3-phospho-D-glycerate + 2 H+ + 2 reduced ferredoxin
D-glyceraldehyde 3-phosphate + H2O + oxidized benzyl viologen
3-phospho-D-glycerate + H+ + reduced benzyl viologen
D-glyceraldehyde-3-phosphate + H2O + oxidized benzyl viologen
3-phospho-D-glycerate + H+ + reduced benzyl viologen
D-glyceraldehyde-3-phosphate + H2O + oxidized ferredoxin
3-phospho-D-glycerate + H+ + reduced ferredoxin
D-glyceraldehyde-3-phosphate + H2O + oxidized methyl viologen
3-phospho-D-glycerate + reduced methyl viologen + H+
Substrates: -
Products: -
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glyceraldehyde 3-phosphate + H2O + oxidized ferredoxin
glycerate 3-phosphate + H+ + reduced ferredoxin
D-glyceraldehyde 3-phosphate + H2O + 2 oxidized ferredoxin
3-phospho-D-glycerate + 2 H+ + 2 reduced ferredoxin
-
Substrates: -
Products: -
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D-glyceraldehyde 3-phosphate + H2O + 2 oxidized ferredoxin
3-phospho-D-glycerate + 2 H+ + 2 reduced ferredoxin
-
Substrates: the enzyme is involved in the modified Embden-Meyerhof pathway
Products: -
Products: -
?
D-glyceraldehyde 3-phosphate + H2O + oxidized benzyl viologen
3-phospho-D-glycerate + H+ + reduced benzyl viologen
-
Substrates: -
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?
D-glyceraldehyde 3-phosphate + H2O + oxidized benzyl viologen
3-phospho-D-glycerate + H+ + reduced benzyl viologen
Substrates: -
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?
D-glyceraldehyde 3-phosphate + H2O + oxidized benzyl viologen
3-phospho-D-glycerate + H+ + reduced benzyl viologen
Substrates: -
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D-glyceraldehyde-3-phosphate + H2O + oxidized benzyl viologen
3-phospho-D-glycerate + H+ + reduced benzyl viologen
Substrates: only GAPOR catalyzes D-glyceraldehyde-3-phosphate oxidation, catalysis under autotrophic conditions
Products: -
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D-glyceraldehyde-3-phosphate + H2O + oxidized benzyl viologen
3-phospho-D-glycerate + H+ + reduced benzyl viologen
Substrates: is highly specific for glyceraldehyde-3-phosphate
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D-glyceraldehyde-3-phosphate + H2O + oxidized benzyl viologen
3-phospho-D-glycerate + H+ + reduced benzyl viologen
-
Substrates: artificial electron acceptor
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D-glyceraldehyde-3-phosphate + H2O + oxidized benzyl viologen
3-phospho-D-glycerate + H+ + reduced benzyl viologen
Substrates: artificial electron acceptor
Products: -
Products: -
?
D-glyceraldehyde-3-phosphate + H2O + oxidized ferredoxin
3-phospho-D-glycerate + H+ + reduced ferredoxin
-
Substrates: -
Products: -
Products: -
?
D-glyceraldehyde-3-phosphate + H2O + oxidized ferredoxin
3-phospho-D-glycerate + H+ + reduced ferredoxin
Substrates: -
Products: -
Products: -
?
D-glyceraldehyde-3-phosphate + H2O + oxidized ferredoxin
3-phospho-D-glycerate + H+ + reduced ferredoxin
-
Substrates: -
Products: -
Products: -
?
D-glyceraldehyde-3-phosphate + H2O + oxidized ferredoxin
3-phospho-D-glycerate + H+ + reduced ferredoxin
-
Substrates: -
Products: -
Products: -
ir
D-glyceraldehyde-3-phosphate + H2O + oxidized ferredoxin
3-phospho-D-glycerate + H+ + reduced ferredoxin
-
Substrates: -
Products: -
Products: -
?
D-glyceraldehyde-3-phosphate + H2O + oxidized ferredoxin
3-phospho-D-glycerate + H+ + reduced ferredoxin
Substrates: -
Products: -
Products: -
?
D-glyceraldehyde-3-phosphate + H2O + oxidized ferredoxin
3-phospho-D-glycerate + H+ + reduced ferredoxin
Substrates: enzyme is a site for glycolytic regulation
Products: -
Products: -
?
D-glyceraldehyde-3-phosphate + H2O + oxidized ferredoxin
3-phospho-D-glycerate + H+ + reduced ferredoxin
-
Substrates: might have a glycolytic role and functions in place of glyceraldehyde-3-phosphate dehydrogenase and possibly phosphoglycerate kinase
Products: -
Products: -
?
glyceraldehyde + H2O + oxidized ferredoxin
glycerate + H+ + reduced ferredoxin
B9MQI2; B9MQI1
Substrates: -
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Products: -
?
glyceraldehyde + H2O + oxidized ferredoxin
glycerate + H+ + reduced ferredoxin
B9MQI2; B9MQI1
Substrates: -
Products: -
Products: -
?
glyceraldehyde 3-phosphate + H2O + oxidized ferredoxin
glycerate 3-phosphate + H+ + reduced ferredoxin
B9MQI2; B9MQI1
Substrates: -
Products: -
Products: -
?
glyceraldehyde 3-phosphate + H2O + oxidized ferredoxin
glycerate 3-phosphate + H+ + reduced ferredoxin
B9MQI2; B9MQI1
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: does not use glyceraldehyde, acetaldehyde or formaldehyde as substrates
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?
additional information
?
-
Substrates: does not use glyceraldehyde, acetaldehyde or formaldehyde as substrates
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?
additional information
?
-
-
Substrates: enzyme shows high specificity for glyceraldehyde-3-phosphate and does not use glyceraldehyde, acetaldehyde or formaldehyde
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Products: -
?
additional information
?
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Substrates: enzyme shows high specificity for glyceraldehyde-3-phosphate and does not use glyceraldehyde, acetaldehyde or formaldehyde
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme shows high specificity for glyceraldehyde-3-phosphate and does not use glyceraldehyde, acetaldehyde or formaldehyde
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?
additional information
?
-
-
Substrates: no activity with NAD(P)+ as electron acceptor
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?
additional information
?
-
-
Substrates: no activity with NAD(P)+ as electron acceptor
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?
additional information
?
-
-
Substrates: no activity with formaldehyde, propionaldehyde, phenylacetaldehyde, butyraldehyde, crotonaldehyde, acetaldehyde, dihydroxyacetone phosphate, glyceraldehyde, benzaldehyde, glucose, glucose 6-phosphate, or glyoxylate
Products: -
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additional information
?
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Substrates: no activity with formaldehyde, propionaldehyde, phenylacetaldehyde, butyraldehyde, crotonaldehyde, acetaldehyde, dihydroxyacetone phosphate, glyceraldehyde, benzaldehyde, glucose, glucose 6-phosphate, or glyoxylate
Products: -
Products: -
?
additional information
?
-
Substrates: substrate glyceraldehyde-3-phosphate degrades at 60Ā°C by non-enzymatic elimination of the phosphate group to methylglyoxal with a half-life of 6.5 min. Methylglyoxal is not a substrate or inhibitor of GAPOR
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additional information
?
-
-
Substrates: substrate glyceraldehyde-3-phosphate degrades at 60Ā°C by non-enzymatic elimination of the phosphate group to methylglyoxal with a half-life of 6.5 min. Methylglyoxal is not a substrate or inhibitor of GAPOR
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
D-glyceraldehyde 3-phosphate + H2O + 2 oxidized ferredoxin
3-phospho-D-glycerate + 2 H+ + 2 reduced ferredoxin
-
Substrates: the enzyme is involved in the modified Embden-Meyerhof pathway
Products: -
Products: -
?
D-glyceraldehyde-3-phosphate + H2O + oxidized ferredoxin
3-phospho-D-glycerate + H+ + reduced ferredoxin
D-glyceraldehyde-3-phosphate + H2O + oxidized ferredoxin
3-phospho-D-glycerate + H+ + reduced ferredoxin
-
Substrates: -
Products: -
Products: -
?
D-glyceraldehyde-3-phosphate + H2O + oxidized ferredoxin
3-phospho-D-glycerate + H+ + reduced ferredoxin
-
Substrates: -
Products: -
Products: -
?
D-glyceraldehyde-3-phosphate + H2O + oxidized ferredoxin
3-phospho-D-glycerate + H+ + reduced ferredoxin
-
Substrates: -
Products: -
Products: -
ir
D-glyceraldehyde-3-phosphate + H2O + oxidized ferredoxin
3-phospho-D-glycerate + H+ + reduced ferredoxin
-
Substrates: -
Products: -
Products: -
?
D-glyceraldehyde-3-phosphate + H2O + oxidized ferredoxin
3-phospho-D-glycerate + H+ + reduced ferredoxin
Substrates: enzyme is a site for glycolytic regulation
Products: -
Products: -
?
D-glyceraldehyde-3-phosphate + H2O + oxidized ferredoxin
3-phospho-D-glycerate + H+ + reduced ferredoxin
-
Substrates: might have a glycolytic role and functions in place of glyceraldehyde-3-phosphate dehydrogenase and possibly phosphoglycerate kinase
Products: -
Products: -
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
molybdopterin
content of Mo-GAPOR expressed in Escherichia coli strain BL21(DE3) is estimated to be 0.35 g-atoms per mol of protein
[4Fe-4S]-center
B9MQI2; B9MQI1
large subunit GOR-L contains one iron-sulfur [4Fe-4S] cluster, small subunit GOR-S contains four [4Fe-4S] cluster
additional information
GAPOR obtained from cells grown in medium containing tungsten and molybdenum or in medium without added tungsten and molybdenum do not display any activity
-
additional information
-
GAPOR obtained from cells grown in medium containing tungsten and molybdenum or in medium without added tungsten and molybdenum do not display any activity
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Mo5+
molybdenum can in be incorporated, Mo(V) signal is observed in electron paramagnetic resonance
S2-
Mo-GAPOR expressed in Escherichia coli strain BL21(DE3) is estimated to contain 6.1 g-atoms of acid-labile sulfide per mol of protein
Tungsten
Tungsten
B9MQI2; B9MQI1
large subunit GOR-L contains a single tungstopterin site and one iron-sulfur [4Fe-4S] cluster
Tungsten
-
0.85 tungsten g-atoms per mol of enzyme, part of a tungsten-molybdopterin cofactor
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
D-glyceraldehyde 3-phosphate
partial substrate inhibition, inhibition is alleviated completely by a 1M NaCl resulting in increased enzyme activity at high substrate concentrations
D-Glyceraldehyde-3-phosphate
recombinant GAPOR is posttranscriptionally regulated as it exhibits pronounced and irreversible substrate inhibition. Inhibition is independent of benzyl viologen
O2
reversibly inactivates GAPOR purified from M9/Mo+ cultures. GAPOR activity of crude lysates is irreversibly inactivated
Dithionite
-
50% inhibition at 3 mM, pH 8.0; O2-scavenger; reversible by 70%
additional information
B9MQI2; B9MQI1
bifunctional phosphoglycerate kinase/triose-phosphate isomerase is a strong inhibitor of GOR
-
additional information
addition of 0.001 mM AMP, NADH, or NADPH has no effect on GAPOR activity
-
additional information
-
addition of 0.001 mM AMP, NADH, or NADPH has no effect on GAPOR activity
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
isopropyl-beta-D-thiogalactopyranoside
1 mM induces cultures at the exponential phase of growth
L-cysteine
reversibly activates GAPOR purified from M9/Mo+ cultures
NaCl
enzyme shows partial substrate inhibition, inhibition is alleviated completely by a 1M NaCl resulting in increased enzyme activity at high substrate concentrations
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.28
D-glyceraldehyde 3-phosphate
-
cosubstrate: benzyl viologen, 50Ā°C, pH not specified in the publication
0.028
D-Glyceraldehyde-3-phosphate
-
with ferredoxin as electron acceptor, pH 8.4, 70Ā°C
0.043
D-Glyceraldehyde-3-phosphate
-
with benzyl viologen as electron acceptor, pH 8.4, 70Ā°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.07
-
substrate: D-glyceraldehyde 3-phosphate (cosubstrate: benzyl viologen), 50Ā°C, pH not specified in the publication, enzyme from starch-grown cells
1.8
maximum specific activity of protein for Mo-GAPOR expressed in Escherichia coli strain BL21(DE3)
120
Mo-GAPOR purified from Escherichia coli strain Rosetta-gami 2(DE3)
17
25
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
B9MQI2 i.e. large subunit GOR-L, B9MQI1 i.e. 4Fe-4S ferredoxin iron-sulfur binding domain protein, GOR-S
B9MQI2; B9MQI1
UniProt
brenda
B9MQI2 i.e. large subunit GOR-L, B9MQI1 i.e. 4Fe-4S ferredoxin iron-sulfur binding domain protein, GOR-S
B9MQI2; B9MQI1
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
specific activity is 10fold higher in starch-grown cells than in lactate-grown cells
brenda
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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
metabolism
physiological function
metabolism
extracts of maltose/yeast extract/nitrate-grown cells contain all enzyme activities of a modified Embden-Meyerhof pathway, including ATP-dependent glucokinase, phosphoglucose isomerase, ATP-dependent 6-phosphofructokinase, fructose-1,6-phosphate aldolase, triose-phosphate isomerase, glyceraldehyde-3-phosphate ferredoxin oxidoreductase, phosphoglycerate mutase, enolase and pyruvate kinase
metabolism
-
extracts of maltose/yeast extract/nitrate-grown cells contain all enzyme activities of a modified Embden-Meyerhof pathway, including ATP-dependent glucokinase, phosphoglucose isomerase, ATP-dependent 6-phosphofructokinase, fructose-1,6-phosphate aldolase, triose-phosphate isomerase, glyceraldehyde-3-phosphate ferredoxin oxidoreductase, phosphoglycerate mutase, enolase and pyruvate kinase
-
physiological function
-
the enzyme is involved in the modified Embden-Meyerhof pathway
physiological function
B9MQI2; B9MQI1
deletion of either subunit results in a distinct growth phenotype on both C5 and C6 sugars, with an increased lag phase, but higher cell densities. GOR functions in parallel with the conventional glyceraldehyde-3-phosphate dehydrogenase
physiological function
either of the two enzymes, ferredoxin-dependent glyceraldehyde-3-phosphate ferredoxin oxidoreductase (GAPOR) or NADP+-dependent non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase (GAPN), involved in the modified Embden-Meyerhof glycolytic pathway can be deleted individually without impacting viability, albeit with differences in native fermentation product profiles. Pyrococcus furiosus is viable in the gluconeogenic direction (growth on pyruvate or peptides plus elemental sulfur) in a DAPOR/GAPN double deletion strain.
physiological function
-
deletion of either subunit results in a distinct growth phenotype on both C5 and C6 sugars, with an increased lag phase, but higher cell densities. GOR functions in parallel with the conventional glyceraldehyde-3-phosphate dehydrogenase
-
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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). GAPOR_PYRFU
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
653
0
73948
Swiss-Prot
-
A0A811TCR5_9EURY
628
0
70156
TrEMBL
-
E8R8U8_DESM0
Desulfurococcus mucosus (strain ATCC 35584 / DSM 2162 / JCM 9187 / O7/1)
654
0
73957
TrEMBL
-
A4WHD7_PYRAR
Pyrobaculum arsenaticum (strain DSM 13514 / JCM 11321 / PZ6)
616
0
69367
TrEMBL
-
A4FXX8_METM5
Methanococcus maripaludis (strain C5 / ATCC BAA-1333)
613
0
70911
TrEMBL
-
S0FU45_9DELT
629
0
71244
TrEMBL
-
A3DPV6_STAMF
Staphylothermus marinus (strain ATCC 43588 / DSM 3639 / JCM 9404 / F1)
658
0
75595
TrEMBL
-
A0A811TI29_9EURY
259
0
29569
TrEMBL
-
A3MTX3_PYRCJ
Pyrobaculum calidifontis (strain DSM 21063 / JCM 11548 / VA1)
629
0
70612
TrEMBL
-
A0A7R9N0X8_9EURY
629
0
70617
TrEMBL
-