EC Explorer

[browse EC tree] - [search]

EC 1.6.1.4 Details

show Brenda entry

EC number

1.6.1.4

Accepted name

NAD(P)⁺ transhydrogenase (ferredoxin)

Reaction

NADH + H⁺ + 2 NADP⁺ + 2 reduced ferredoxin [iron-sulfur] cluster = NAD⁺ + 2 NADPH + 2 oxidized ferredoxin [iron-sulfur] cluster

Other name(s)

NADH-dependent reduced ferredoxin:NADP⁺ oxidoreductase, Nfn, nfnAB (gene names)

Systematic name

NADH:NADP⁺, ferredoxin oxidoreductase

Comment

The iron-sulfur flavoprotein complex, originally isolated from the bacterium Clostridium kluyveri, couples the exergonic reduction of NADP⁺ with reduced ferredoxin and the endergonic reduction of NADP⁺ with NADH.

History

created 2015

EC Tree

1 Oxidoreductases

1.1 Acting on the CH-OH group of donors

1.2 Acting on the aldehyde or oxo group of donors

1.2.1 With NAD⁺ or NADP⁺ as acceptor

1.2.2 With a cytochrome as acceptor

1.2.3 With oxygen as acceptor

1.2.4 With a disulfide as acceptor

1.2.5 With a quinone or similar compound as acceptor

1.2.7 With an iron-sulfur protein as acceptor

1.2.98 With other, known, physiological acceptors

1.2.99 With unknown physiological acceptors

1.3 Acting on the CH-CH group of donors

1.4 Acting on the CH-NH₂ group of donors

1.5 Acting on the CH-NH group of donors

1.6 Acting on NADH or NADPH

1.6.1 With NAD⁺ or NADP⁺ as acceptor

1.6.1.1 NAD(P)⁺ transhydrogenase (Si-specific)

1.6.1.2 NAD(P)⁺ transhydrogenase (Re/Si-specific)

1.6.1.3 NAD(P)⁺ transhydrogenase

1.6.1.4 NAD(P)⁺ transhydrogenase (ferredoxin)

1.6.1.5 proton-translocating NAD(P)⁺ transhydrogenase

1.6.2 With a heme protein as acceptor

1.6.3 With oxygen as acceptor

1.6.4 With a disulfide as acceptor (deleted sub-subclass)

1.6.5 With a quinone or similar compound as acceptor

1.6.6 With a nitrogenous group as acceptor

1.6.6.1 created 1961, deleted 2002

1.6.6.2 created 1961, deleted 2002

1.6.6.3 created 1961, deleted 2002

1.6.6.4 created 1961, deleted 2002

1.6.6.5 created 1961, deleted 1964

1.6.6.6 created 1961, deleted 2002

1.6.6.7 created 1961, deleted 2002

1.6.6.8 created 1965, deleted 2002

1.6.6.9 trimethylamine-N-oxide reductase

1.6.6.10 created 1972, deleted 2002

1.6.6.11 created 1972, deleted 2002

1.6.6.12 created 1989, deleted 2002

1.6.6.13 created 1989, deleted 2002

1.6.7 With an iron-sulfur protein as acceptor (deleted sub-subclass)

1.6.8 With a flavin as acceptor (deleted sub-subclass)

1.6.99 With unknown physiological acceptors

1.7 Acting on other nitrogenous compounds as donors

1.8 Acting on a sulfur group of donors

1.9 Acting on a heme group of donors

1.10 Acting on diphenols and related substances as donors

1.11 Acting on a peroxide as acceptor

1.12 Acting on hydrogen as donor

1.13 Acting on single donors with incorporation of molecular oxygen (oxygenases)

1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen

1.15 Acting on superoxide as acceptor

1.16 Oxidizing metal ions

1.17 Acting on CH or CH₂ groups

1.17.1 With NAD⁺ or NADP⁺ as acceptor

1.17.2 With a cytochrome as acceptor

1.17.3 With oxygen as acceptor

1.17.4 With a disulfide as acceptor

1.17.5 With a quinone or similar compound as acceptor

1.17.7 With an iron-sulfur protein as acceptor

1.17.8 With a flavin as acceptor

1.17.9 With a copper protein as acceptor

1.17.98 With other, known, physiological acceptors

1.17.99 With unknown physiological acceptors

1.18 Acting on iron-sulfur proteins as donors

1.19 Acting on reduced flavodoxin as donor

1.20 Acting on phosphorus or arsenic in donors

1.20.1 With NAD⁺ or NADP⁺ as acceptor

1.20.2 With a cytochrome as acceptor

1.20.4 With disulfide as acceptor

1.20.9 With a copper protein as acceptor

1.20.98 With other, known, physiological acceptors

1.20.99 With unknown physiological acceptors

1.21 Catalysing the reaction X-H + Y-H = X-Y

1.22 Acting on halogen in donors

1.23 Reducing C-O-C group as acceptor

1.97 Other oxidoreductases

1.98 Enzymes using H₂ as reductant (deleted subclass)

1.99 Other enzymes using O₂ as oxidant (deleted subclass)

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)