Information on EC 1.8.7.2 - ferredoxin:thioredoxin reductase

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The expected taxonomic range for this enzyme is: Eukaryota, Archaea, Bacteria

EC NUMBER
COMMENTARY hide
1.8.7.2
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RECOMMENDED NAME
GeneOntology No.
ferredoxin:thioredoxin reductase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2 reduced ferredoxin + thioredoxin disulfide = 2 oxidized ferredoxin + thioredoxin + 2 H+
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
ferredoxin:thioredoxin disulfide oxidoreductase
The enzyme contains a [4Fe-4S] cluster and internal disulfide. It forms a mixed disulfide with thioredoxin on one side, and docks ferredoxin on the other side, enabling two one-electron transfers. The reduced thioredoxins generated by the enzyme activate the Calvin cycle enzymes EC 3.1.3.11 (fructose-bisphosphatase), EC 3.1.3.37 (sedoheptulose-bisphosphatase) and EC 2.7.1.19 (phosphoribulokinase) as well as other chloroplast enzymes by disulfide reduction.
CAS REGISTRY NUMBER
COMMENTARY hide
65589-57-3
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
chimeric protein containing a plant-type ferredoxin/thioredoxin reductase-like catalytic domain in the N-terminal region and a bacterial-like rubredoxin domain in the C-terminal region
UniProt
Manually annotated by BRENDA team
chimeric protein containing a plant-type ferredoxin/thioredoxin reductase-like catalytic domain in the N-terminal region and a bacterial-like rubredoxin domain in the C-terminal region
UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
additional information
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role for Fe-S clusters in the enzyme mechanism involving both the stabilization of a thiyl radical intermediate and cluster site-specific chemistry involving a bridging sulfide
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
reduced ferredoxin + thioredoxin disulfide
2 oxidized ferredoxin + thioredoxin + 2 H+
show the reaction diagram
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?
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4Fe-4S-center
Ferredoxin
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ferredoxin-thioredoxin reductase forms an electrostatically stabilized 1:1 complex with ferredoxin. Chemical modification of three or four carboxyl groups on ferredoxin has little effect on its interaction with ferredoxin-thioredoxin reductase. The ferredoxin domain that binds ferredoxin-thioredoxin reductase is not completely identical to that involved in binding other ferredoxin-dependent enzymes
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Iron
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presence of an S = 0 [4Fe-4S]2+ cluster with complete cysteinyl-S coordination that cannot be reduced at potentials down to -650 mV, but can be oxidized by ferricyanide to an S = 1/2 [4Fe-4S]3+ state. The midpoint potential for the [4Fe-4S]3+/2+ couple is estimated to be +420 mV versus NHE. Results argue against a role for the cluster in mediating electron transport from ferredoxin to the active-site disulfide and suggest an alternative role for the cluster in stabilizing the one-electron-reduced intermediate. A mechanistic scheme is proposed involving sequential one-electron redox processes with the role of the [4Fe-4S]2+ cluster being to stabilize the thiyl radical formed by the initial one-electron reduction of the active-site disulfide
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
N-ethylmaleimide
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.7 - 1.8
Ferredoxin
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.3
catalytic subunit, calculated
5.4
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subunit A, calculated
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
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transcripts of the catalytic subunit FTR-c are detected in all tissues examined, including roots, leaves, flowers, fruits, and seeds
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Synechocystis sp. (strain PCC 6803 / Kazusa)
Synechocystis sp. (strain PCC 6803 / Kazusa)
Synechocystis sp. (strain PCC 6803 / Kazusa)
Synechocystis sp. (strain PCC 6803 / Kazusa)
Synechocystis sp. (strain PCC 6803 / Kazusa)
Synechocystis sp. (strain PCC 6803 / Kazusa)
Synechocystis sp. (strain PCC 6803 / Kazusa)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
31000
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gel filtration, recombinant protein complex
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
alpha/beta, peptide mapping for localization of labeled cysteinyl residues, overview
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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presence of a N-terminal extension in subunit A
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
to 2.8 A resolution, primitive cubic space group P23 or P213
Mössbauer spectroscopy study of both the as-purified and N-ethylmaleimide-modified forms of FTR demonstrate the presence of a unique iron site in the [4Fe-4S] cluster and suggest that site-specific cluster chemistry, involving the formation of a five-coordinate Fe site with two cysteinate ligands, occurs during catalytic cycling of FTR
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mapping of the binding sites of ferredoxin for FTR by NMR using a gallium-substituted structural analog of ferredoxin. The interaction of erredoxin with FTR is in the slow to intermediate exchange regime. All of the residues with large chemical shift changes except I51 are located near the [2Fe-2S] loop
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paramagnetic NMR spectroscopy study on the ternary protein complex of ferredoxin, ferredoxin:thioredoxin reductase, and thioredoxin. FTR uses distinct sites to bind ferredoxin and thioredoxin simultaneously to form a noncovalent ternary complex. Either a modest or major rotational movement of thioredoxin must take place when the noncovalent binary complex proceeds to the covalent complex
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structures of FTR in both its one- and its two-electron-reduced intermediate states and of four complexes in the pathway. In the first complex of the pathway, ferredoxin-FTR, the ferredoxin [2Fe-2S] cluster is positioned suitably for electron transfer to the FTR [4Fe-4S] center. After the transfer of one electron, an intermediate is formed in which one sulfur atom of the FTR active site is free to attack a disulphide bridge in thioredoxin and the other sulfur atom forms a fifth ligand for an iron atom in the FTR [4Fe-4S] center. Ferredoxin then delivers a second electron that cleaves the FTR-thioredoxin heterodisulfide bond, which occurs in the ferredoxin-FTR-thioredoxin complex. In this structure, the redox centers of the three proteins are aligned to maximize the efficiency of electron transfer from the Fdx [2Fe-2S] cluster to the active-site disulfide of thioredoxin
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme from leaves
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
catalytic subunit
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expression in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C27S
mutation in truncated, stabilized FTR mutant lacking 24 N-terminal amino acids. Mutant C27S is perfectly capable of activating FBPase and shows a thioredoxin f-concentration dependency comparable to the FTR truncation mutant
C84S
mutation in truncated, stabilized FTR mutant lacking 24 N-terminal amino acids. Mutant C84S is produced at about the same level as the WT protein, it is extremely labile and disintegrates very rapidly during the first steps of purifiation
C57S
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active site mutant, inactive. Spectral analysis indicates a reduced Fe-S cluster which can be reduced by dithionite. Stable protein, forms stable covalent heteroduplexes with active-site mutant thioredoxins Trx f C49S or Trx m C40S
C87A
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active site mutant, inactive. Spectral analysis indicates an oxidized Fe-S cluster. Mutants is unable to form stable covalent heteroduplexes with active-site mutant thioredoxins Trx f C49S or Trx m C40S
additional information
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
isolation of gallium-substituted Fd through refolding the apoprotein in a refolding buffer containing excess Ga(III)
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
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dicistronic construct for the heterologous expression in Escherichia coli. The coding sequences for the two mature subunits have been inserted in tandem into the expression vector. The dicistronic construct is correctly translated yielding soluble, perfectly functional FTR. The recombinant enzyme is composed of both subunits, contains the correctly inserted FeS cluster and is indistinguishable from the enzyme isolated from leaves in its capacity to activate chloroplast fructose-1,6-bisphosphatase
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