1.8.7.2: ferredoxin:thioredoxin reductase
This is an abbreviated version!
For detailed information about ferredoxin:thioredoxin reductase, go to the full flat file.
Word Map on EC 1.8.7.2
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1.8.7.2
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thioredoxins
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chloroplast
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spinach
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redox-active
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reductases
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epr
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fe-s
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light-dependent
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one-electron-reduced
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two-electron
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iron-sulfur
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raman
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one-electron
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variable-temperature
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heterodisulfide
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dithiol
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methanosarcina
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synthesis
- 1.8.7.2
- thioredoxins
- chloroplast
- spinach
-
redox-active
- reductases
- epr
- fe-s
-
light-dependent
-
one-electron-reduced
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two-electron
-
iron-sulfur
-
raman
-
one-electron
-
variable-temperature
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heterodisulfide
- dithiol
-
methanosarcina
- synthesis
Reaction
2 reduced ferredoxin + = 2 oxidized ferredoxin + + 2 H+
Synonyms
Fd-thioredoxin reductase, Fd:TRX reductase, FdR, Fdx flavin-thioredoxin reductase, Fdx-dependent thioredoxin reductase, FDX-dependent TRX reductase, ferredoxin disulfide reductase, ferredoxin-dependent thioredoxin reductase, ferredoxin-thioredoxin reductase, FFTR, FTR, FTRc, glr0719, GvDTR, iron-sulfur ferredoxin-dependent thioredoxin reductase, Ma_1659, protein modulase
ECTree
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Subunits
Subunits on EC 1.8.7.2 - ferredoxin:thioredoxin reductase
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dimer
alpha/beta, peptide mapping for localization of labeled cysteinyl residues, overview
heterodimer
homodimer
additional information
?
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x * ? + x * 12669, subunit A, without a known catalytic function, calculated
?
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x * ? + x * 10939, variable subunit, without known catalytic function, calculated
GvDTR is a homodimer with each monomer composed of two conserved Rossmann-type modules that form the FAD-binding and redox-active disulfide domains
homodimer
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GvDTR is a homodimer with each monomer composed of two conserved Rossmann-type modules that form the FAD-binding and redox-active disulfide domains
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protein modulase is a complex protein composed of ferredoxin/thioredoxin reductase, ferredoxin, and thioredoxin. Buffer ionic strength affects the interactions among these proteins and in part determines the fate of the protein modulase complex in vitro. The ferredoxin and thioredoxin active in light modulation are not free in solution
additional information
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amino acid sequence of the catalytic subunit. Six of the eight cysteine residues are clustered as Cys-Pro-Cys and Cys-His-Cys groups. Cysl9 and Cys27 are free cysteines with no catalytic function, Cys54 and Cys84 constitute the redox-active disulfide bridge of the active site, and the remaining four, Cys52, Cys71, Cys73, and Cys82 bind the Fe-S cluster
additional information
amino acid sequence of the catalytic subunit. Six of the eight cysteine residues are clustered as Cys-Pro-Cys and Cys-His-Cys groups. Cysl9 and Cys27 are free cysteines with no catalytic function, Cys54 and Cys84 constitute the redox-active disulfide bridge of the active site, and the remaining four, Cys52, Cys71, Cys73, and Cys82 bind the Fe-S cluster