BRENDA - Enzyme Database show
show all sequences of 1.8.7.2

Ferredoxinthioredoxin reductase (FTR) links the regulation of oxygenic photosynthesis to deeply rooted bacteria

Balsera, M.; Uberegui, E.; Susanti, D.; Schmitz, R.; Mukhopadhyay, B.; Schürmann, P.; Buchanan, B.; Planta 237, 619-635 (2013)

Data extracted from this reference:

Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
oxidized ferredoxin + thioredoxin + H+
Synechocystis sp. PCC 6803
-
reduced ferredoxin + thioredoxin disulfide
-
-
?
oxidized ferredoxin + thioredoxin + H+
Amblyomma maculatum
-
reduced ferredoxin + thioredoxin disulfide
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Amblyomma maculatum
-
-
-
no activity in Gloeobacter violaceus
-
-
-
Synechocystis sp. PCC 6803
Q55389
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
oxidized ferredoxin + thioredoxin + H+
-
743549
Synechocystis sp. PCC 6803
reduced ferredoxin + thioredoxin disulfide
-
-
-
?
oxidized ferredoxin + thioredoxin + H+
-
743549
Amblyomma maculatum
reduced ferredoxin + thioredoxin disulfide
-
-
-
?
Subunits
Subunits
Commentary
Organism
heterodimer
-
Amblyomma maculatum
heterodimer
-
Synechocystis sp. PCC 6803
Cofactor
Cofactor
Commentary
Organism
Structure
Ferredoxin
-
Amblyomma maculatum
Ferredoxin
-
Synechocystis sp. PCC 6803
[4Fe-4S]-center
-
Amblyomma maculatum
[4Fe-4S]-center
-
Synechocystis sp. PCC 6803
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
Ferredoxin
-
Amblyomma maculatum
Ferredoxin
-
Synechocystis sp. PCC 6803
[4Fe-4S]-center
-
Amblyomma maculatum
[4Fe-4S]-center
-
Synechocystis sp. PCC 6803
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
oxidized ferredoxin + thioredoxin + H+
Synechocystis sp. PCC 6803
-
reduced ferredoxin + thioredoxin disulfide
-
-
?
oxidized ferredoxin + thioredoxin + H+
Amblyomma maculatum
-
reduced ferredoxin + thioredoxin disulfide
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
oxidized ferredoxin + thioredoxin + H+
-
743549
Synechocystis sp. PCC 6803
reduced ferredoxin + thioredoxin disulfide
-
-
-
?
oxidized ferredoxin + thioredoxin + H+
-
743549
Amblyomma maculatum
reduced ferredoxin + thioredoxin disulfide
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
heterodimer
-
Amblyomma maculatum
heterodimer
-
Synechocystis sp. PCC 6803
Other publictions for EC 1.8.7.2
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
741861
Yoshida
Distinct electron transfer fr ...
Arabidopsis thaliana
Biochem. J.
474
1347-1360
2017
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1
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10
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2
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10
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743739
Okegawa
Expression of spinach ferredo ...
Spinacia oleracea
Protein Expr. Purif.
121
46-51
2016
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1
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1
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741911
Kumar
Structural and biochemical ch ...
Methanosarcina acetivorans
Biochemistry
54
3122-3128
2015
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1
1
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3
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1
1
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743165
Smiri
The role of ferredoxinthiored ...
Cicer arietinum
J. Plant Physiol.
171
1664-1670
2014
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1
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1
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1
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743317
Wang
-
Ferredoxinthioredoxin reducta ...
Arabidopsis thaliana
Mol. Plant
7
1586-1590
2014
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1
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1
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1
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1
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1
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1
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1
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1
1
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1
1
-
-
-
743549
Balsera
Ferredoxinthioredoxin reducta ...
Amblyomma maculatum, no activity in Gloeobacter violaceus, Synechocystis sp. PCC 6803
Planta
237
619-635
2013
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2
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5
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2
2
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4
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4
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2
2
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723858
Kumar
Expression, purification, crys ...
Methanosarcina acetivorans, Methanosarcina acetivorans DSM 2834
Acta Crystallogr. Sect. F
67
775-778
2011
-
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1
1
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702104
Lim
Silencing of SlFTR-c, the cata ...
Solanum lycopersicum
Biochem. Biophys. Res. Commun.
399
750-754
2010
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4
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6
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6
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1
1
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702253
Walters
Role of histidine-86 in the ca ...
Synechocystis sp.
Biochemistry
48
1016-1024
2009
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1
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3
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704186
Xu
Ternary protein complex of fer ...
Synechocystis sp.
J. Am. Chem. Soc.
131
17576-17582
2009
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689503
Hishiya
Binary reducing equivalent pat ...
Synechocystis sp.
Plant Cell Physiol.
49
11-18
2008
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1
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1
1
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705878
Dai
Structural snapshots along the ...
Synechocystis sp.
Nature
448
92-96
2007
-
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1
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703694
Xu
Ferredoxin/ferredoxin-thioredo ...
Synechocystis sp.
FEBS Lett.
580
6714-6720
2006
-
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-
1
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1
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1
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1
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704409
Glauser
Characterization of ferredoxin ...
Synechocystis sp.
J. Biol. Chem.
279
16662-16669
2004
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3
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2
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706103
Keryer
Characterization of Arabidopsi ...
Arabidopsis thaliana
Photosyn. Res.
79
265-274
2004
-
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4
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1
1
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703693
Manieri
N-terminal truncation of the v ...
Spinacia oleracea
FEBS Lett.
549
167-170
2003
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3
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704156
Jameson
Spectroscopic evidence for sit ...
Spinacia oleracea
J. Am. Chem. Soc.
125
1146-1147
2003
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706343
Gaymard
A dicistronic construct for th ...
Spinacia oleracea
Plant Sci.
158
107-113
2000
-
1
1
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1
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2
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1
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702198
Staples
Role of the [Fe4S4] cluster in ...
Spinacia oleracea
Biochemistry
37
4612-4620
1998
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1
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1
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4
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702192
Staples
The nature and properties of t ...
Spinacia oleracea
Biochemistry
35
11425-11434
1996
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1
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2
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4
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1
1
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703528
Iwadate
Amino acid sequence of the mai ...
Zea mays
Eur. J. Biochem.
241
121-125
1996
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1
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4
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2
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702397
Salamon
The oxidation-reduction proper ...
Spinacia oleracea
Biochim. Biophys. Acta
1230
114-118
1995
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1
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2
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1
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703527
Chow
Amino acid sequence of spinach ...
Spinacia oleracea
Eur. J. Biochem.
231
149-156
1995
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-
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1
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1
1
1
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3
-
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3
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1
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1
1
1
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3
-
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1
-
1
1
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703525
Iwadate
Amino acid sequence of spinach ...
Spinacia oleracea
Eur. J. Biochem.
223
465-471
1994
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1
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