Information on EC 1.2.1.93 - formate dehydrogenase (NAD+, ferredoxin)

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The expected taxonomic range for this enzyme is: Gottschalkia acidurici

EC NUMBER
COMMENTARY hide
1.2.1.93
-
RECOMMENDED NAME
GeneOntology No.
formate dehydrogenase (NAD+, ferredoxin)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2 formate + NAD+ + 2 oxidized ferredoxin [iron-sulfur] cluster = 2 CO2 + NADH + H+ + 2 reduced ferredoxin [iron-sulfur] cluster
show the reaction diagram
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-
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SYSTEMATIC NAME
IUBMB Comments
formate:NAD+, oxidized ferredoxin oxidoreductase
The enzyme complex, isolated from the bacterium Gottschalkia acidurici, couples the reduction of NAD+ and the reduction of ferredoxin with formate via flavin-based electron bifurcation.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
K0B3A3: formate dehydrogenase subunit, K0AXR5: subunit HylA, K0B622: subunit HylB, K0B468: subunit HylC
K0B3A3 and K0AXR5 and K0B622 and K0B468
UniProt
Manually annotated by BRENDA team
K0B3A3: formate dehydrogenase subunit, K0AXR5: subunit HylA, K0B622: subunit HylB, K0B468: subunit HylC
K0B3A3 and K0AXR5 and K0B622 and K0B468
UniProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
formate + 2 NAD+ + 2 oxidized ferredoxin iron-sulfur cluster
CO2 + 2 NADH + 2 reduced ferredoxin iron-sulfur cluster
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
formate + 2 NAD+ + 2 oxidized ferredoxin iron-sulfur cluster
CO2 + 2 NADH + 2 reduced ferredoxin iron-sulfur cluster
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Fe-S center
K0B3A3 and K0AXR5 and K0B622 and K0B468
the enzyme contains iron-sulfur clusters
FMN
K0B3A3 and K0AXR5 and K0B622 and K0B468
enzyme preparation contains FMN
NAD+
K0B3A3 and K0AXR5 and K0B622 and K0B468
NADP+ can not substitute for NAD+
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
K0B3A3 and K0AXR5 and K0B622 and K0B468
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
18400
K0B3A3 and K0AXR5 and K0B622 and K0B468
x * 99000 (formate dehydrogenase subunit FdhF2) + x * 68000 (HylB) + x * 35900 (HylA) + x * 18400 (HylC), SDS-PAGE, calculated from sequence
35900
K0B3A3 and K0AXR5 and K0B622 and K0B468
x * 99000 (formate dehydrogenase subunit FdhF2) + x * 68000 (HylB) + x * 35900 (HylA) + x * 18400 (HylC), SDS-PAGE, calculated from sequence
68000
K0B3A3 and K0AXR5 and K0B622 and K0B468
x * 99000 (formate dehydrogenase subunit FdhF2) + x * 68000 (HylB) + x * 35900 (HylA) + x * 18400 (HylC), SDS-PAGE, calculated from sequence
99000
K0B3A3 and K0AXR5 and K0B622 and K0B468
x * 99000 (formate dehydrogenase subunit FdhF2) + x * 68000 (HylB) + x * 35900 (HylA) + x * 18400 (HylC), SDS-PAGE, calculated from sequence
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
-
K0B3A3 and K0AXR5 and K0B622 and K0B468