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Information on EC 1.3.2.4 - fumarate reductase (cytochrome)
for references in articles please use BRENDA:EC1.3.2.4
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EC Tree 1 Oxidoreductases
1.3 Acting on the CH-CH group of donors
1.3.2 With a cytochrome as acceptor
1.3.2.4 fumarate reductase (cytochrome)
IUBMB Comments
Contains a non-covalently bound FAD cofactor and four heme c groups. The enzyme, characterized from the bacterium Shewanella frigidimarina, is a soluble periplasmic protein that functions as a terminal electron acceptor during anaerobic growth. The direct electron donor is the membrane-bound tetraheme c-type cytochrome CymA (EC 7.1.1.8, quinol—cytochrome-c reductase), which receives the electrons from the membrane quinol pool.
The enzyme appears in viruses and cellular organisms
showSynonyms
FCC, fcc3, fccA, flavocytochrome c, Flavocytochrome c3, flavocytochrome c3 fumarate reductase, fumarate reductase, fumarate reductases, Ifc3, SFR, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
FCC
fcc3
fccA
flavocytochrome c
Flavocytochrome c3
flavocytochrome c3 fumarate reductase
fumarate reductase
fumarate reductases
Ifc3
fcc3
-
-
-
-
fccA
-
-
-
-
Flavocytochrome c3
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
succinate + 2 ferricytochrome c = fumarate + 2 ferrocytochrome c
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
succinate:ferricytochrome-c oxidoreductase
Contains a non-covalently bound FAD cofactor and four heme c groups. The enzyme, characterized from the bacterium Shewanella frigidimarina, is a soluble periplasmic protein that functions as a terminal electron acceptor during anaerobic growth. The direct electron donor is the membrane-bound tetraheme c-type cytochrome CymA (EC 7.1.1.8, quinol---cytochrome-c reductase), which receives the electrons from the membrane quinol pool.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
fumarate + reduced acceptor
succinate + oxidized acceptor
-
Substrates: -
Products: -
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?
succinate + oxidized 2,6-dichlorophenolindophenol
fumarate + reduced 2,6-dichlorophenolindophenol
fumarate + 2 ferrocytochrome c
succinate + 2 ferricytochrome c
Substrates: -
Products: -
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?
fumarate + 2 ferrocytochrome c
succinate + 2 ferricytochrome c
Substrates: -
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?
fumarate + 2 ferrocytochrome c
succinate + 2 ferricytochrome c
Substrates: -
Products: -
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ir
fumarate + 2 ferrocytochrome c
succinate + 2 ferricytochrome c
-
Substrates: -
Products: -
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?
fumarate + 2 ferrocytochrome c
succinate + 2 ferricytochrome c
Shewanella putrefaciens NCIMB400
Substrates: -
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ir
fumarate + 2 ferrocytochrome c
succinate + 2 ferricytochrome c
Shewanella putrefaciens NCMB 400
-
Substrates: -
Products: -
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?
fumarate + ferrocytochrome c
succinate + ferricytochrome c
Substrates: -
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?
fumarate + ferrocytochrome c
succinate + ferricytochrome c
Substrates: -
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?
fumarate + reduced methyl viologen
succinate + oxidized methyl viologen
Substrates: -
Products: -
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?
fumarate + reduced methyl viologen
succinate + oxidized methyl viologen
-
Substrates: -
Products: -
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?
fumarate + reduced methyl viologen
succinate + oxidized methyl viologen
Substrates: -
Products: -
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?
fumarate + reduced methyl viologen
succinate + oxidized methyl viologen
Substrates: -
Products: -
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?
fumarate + reduced methyl viologen
succinate + oxidized methyl viologen
Substrates: -
Products: -
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?
fumarate + reduced methyl viologen
succinate + oxidized methyl viologen
-
Substrates: -
Products: -
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?
fumarate + reduced methyl viologen
succinate + oxidized methyl viologen
Substrates: -
Products: -
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?
fumarate + reduced methyl viologen
succinate + oxidized methyl viologen
Substrates: -
Products: -
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?
fumarate + reduced methyl viologen
succinate + oxidized methyl viologen
-
Substrates: -
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?
fumarate + reduced methyl viologen
succinate + oxidized methyl viologen
-
Substrates: -
Products: -
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?
fumarate + reduced methyl viologen
succinate + oxidized methyl viologen
Shewanella putrefaciens NCMB 400
-
Substrates: -
Products: -
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?
succinate + 2 ferricytochrome c
fumarate + 2 ferrocytochrome c
-
Substrates: -
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?
succinate + 2 ferricytochrome c
fumarate + 2 ferrocytochrome c
-
Substrates: -
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?
succinate + 2 ferricytochrome c
fumarate + 2 ferrocytochrome c
-
Substrates: -
Products: -
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?
succinate + 2 ferricytochrome c
fumarate + 2 ferrocytochrome c
Shewanella oneidensis MR-1 / ATCC 700550
-
Substrates: -
Products: -
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?
succinate + 2 ferricytochrome c
fumarate + 2 ferrocytochrome c
-
Substrates: -
Products: -
Products: -
?
succinate + 2 ferricytochrome c
fumarate + 2 ferrocytochrome c
Shewanella putrefaciens NCMB 400
-
Substrates: -
Products: -
Products: -
?
succinate + oxidized 2,6-dichlorophenolindophenol
fumarate + reduced 2,6-dichlorophenolindophenol
-
Substrates: -
Products: -
Products: -
?
succinate + oxidized 2,6-dichlorophenolindophenol
fumarate + reduced 2,6-dichlorophenolindophenol
-
Substrates: -
Products: -
Products: -
?
succinate + oxidized 2,6-dichlorophenolindophenol
fumarate + reduced 2,6-dichlorophenolindophenol
-
Substrates: -
Products: -
Products: -
?
succinate + oxidized 2,6-dichlorophenolindophenol
fumarate + reduced 2,6-dichlorophenolindophenol
Shewanella putrefaciens NCMB 400
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: at low electron flux from the cell metabolism, or with high availability of solid terminal electron acceptors, the enzyme will not charge up to a significant extent from CymA and will transfer the electrons to the outer membrane reductases for the reduction of solid phase acceptors. As the electron flux increases, or extracellular electron acceptors become scarce, the enzyme will become increasingly reduced, switching to efficient catalysis of fumarate reduction
Products: -
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?
additional information
?
-
-
Substrates: at low electron flux from the cell metabolism, or with high availability of solid terminal electron acceptors, the enzyme will not charge up to a significant extent from CymA and will transfer the electrons to the outer membrane reductases for the reduction of solid phase acceptors. As the electron flux increases, or extracellular electron acceptors become scarce, the enzyme will become increasingly reduced, switching to efficient catalysis of fumarate reduction
Products: -
Products: -
?
additional information
?
-
-
Substrates: at low electron flux from the cell metabolism, or with high availability of solid terminal electron acceptors, the enzyme will not charge up to a significant extent from CymA and will transfer the electrons to the outer membrane reductases for the reduction of solid phase acceptors. As the electron flux increases, or extracellular electron acceptors become scarce, the enzyme will become increasingly reduced, switching to efficient catalysis of fumarate reduction
Products: -
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?
additional information
?
-
-
Substrates: the enzyme can easily reduce selenite and exhibits negligible adsorption to it. More than 82% of selenite is reduced during 12 h. CymA provides electrons from the quinol pool for selenite reduction to the enzyme. Neither nitrate reductase nor nitrite reductase contribute to selenite reduction
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?
additional information
?
-
-
Substrates: in vitro fumarate reductase FccA is reduced by the cytoplasmic membrane-bound protein CymA
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?
additional information
?
-
-
Substrates: CymA is an efficient electron donor for the soluble fumarate reductase flavocytochrome c3
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?
additional information
?
-
-
Substrates: the enzyme does not reduce nitrite, dimethylsulfoxide, trimethylamine N-oxide, or sulfite
Products: -
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?
additional information
?
-
Shewanella putrefaciens NCMB 400
-
Substrates: the enzyme does not reduce nitrite, dimethylsulfoxide, trimethylamine N-oxide, or sulfite
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
fumarate + reduced acceptor
succinate + oxidized acceptor
-
Substrates: -
Products: -
Products: -
?
fumarate + 2 ferrocytochrome c
succinate + 2 ferricytochrome c
Substrates: -
Products: -
Products: -
?
fumarate + 2 ferrocytochrome c
succinate + 2 ferricytochrome c
Substrates: -
Products: -
Products: -
?
fumarate + 2 ferrocytochrome c
succinate + 2 ferricytochrome c
Substrates: -
Products: -
Products: -
ir
fumarate + 2 ferrocytochrome c
succinate + 2 ferricytochrome c
-
Substrates: -
Products: -
Products: -
?
fumarate + 2 ferrocytochrome c
succinate + 2 ferricytochrome c
Shewanella putrefaciens NCIMB400
Substrates: -
Products: -
Products: -
ir
fumarate + 2 ferrocytochrome c
succinate + 2 ferricytochrome c
Shewanella putrefaciens NCMB 400
-
Substrates: -
Products: -
Products: -
?
fumarate + ferrocytochrome c
succinate + ferricytochrome c
Substrates: -
Products: -
Products: -
?
fumarate + ferrocytochrome c
succinate + ferricytochrome c
Substrates: -
Products: -
Products: -
?
succinate + 2 ferricytochrome c
fumarate + 2 ferrocytochrome c
-
Substrates: -
Products: -
Products: -
?
succinate + 2 ferricytochrome c
fumarate + 2 ferrocytochrome c
-
Substrates: -
Products: -
Products: -
?
succinate + 2 ferricytochrome c
fumarate + 2 ferrocytochrome c
-
Substrates: -
Products: -
Products: -
?
succinate + 2 ferricytochrome c
fumarate + 2 ferrocytochrome c
Shewanella oneidensis MR-1 / ATCC 700550
-
Substrates: -
Products: -
Products: -
?
succinate + 2 ferricytochrome c
fumarate + 2 ferrocytochrome c
-
Substrates: -
Products: -
Products: -
?
succinate + 2 ferricytochrome c
fumarate + 2 ferrocytochrome c
Shewanella putrefaciens NCMB 400
-
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
heme
the N-terminal cytochrome domain contains four covalently bound heme groups
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
fumarate
-
fumarate competitively inhibits selenite reduction by the enzyme
additional information
-
not inhibited by acrylic acid, trans-aconitic acid, and trans-beta-hydromuconic acid
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0007
fumarate
mutant enzyme H61M, with reduced methyl viologen as cosubstrate, at pH 9.0 and 25°C
0.0049
fumarate
mutant enzyme H61M, with reduced methyl viologen as cosubstrate, at pH 7.5 and 25°C
0.005
fumarate
mutant enzyme H61M, with reduced methyl viologen as cosubstrate, at pH 7.2 and 25°C
0.005
fumarate
mutant enzyme H61A, with reduced methyl viologen as cosubstrate, at pH 9.0 and 25°C
0.0051
fumarate
mutant enzyme H61A, with reduced methyl viologen as cosubstrate, at pH 6.0 and 25°C
0.0051
fumarate
mutant enzyme H61A, with reduced methyl viologen as cosubstrate, at pH 7.2 and 25°C
0.0051
fumarate
mutant enzyme H61A, with reduced methyl viologen as cosubstrate, at pH 7.5 and 25°C
0.0053
fumarate
mutant enzyme Q363F/R402A, at pH 7.5 and 25°C
0.0066
fumarate
mutant enzyme Q363F/R402A, at pH 6.0 and 25°C
0.007
fumarate
wild type enzyme, with reduced methyl viologen as cosubstrate, at pH 9.0 and 25°C
0.0099
fumarate
mutant enzyme H61M, with reduced methyl viologen as cosubstrate, at pH 6.0 and 25°C
0.018
fumarate
-
with reduced methyl viologen as cosubstrate, at pH 8.0 and 25°C
0.021
fumarate
-
with reduced methyl viologen as cosubstrate, at pH 7.4, temperature not specified in the publication
0.025
fumarate
wild type enzyme, with reduced methyl viologen as cosubstrate, at pH 7.2 and 25°C
0.025
fumarate
-
with reduced methyl viologen as cosubstrate, at pH 7.2 and 25°C
0.028
fumarate
wild type enzyme, with reduced methyl viologen as cosubstrate, at pH 7.5 and 25°C
0.029
fumarate
-
with reduced methyl viologen as cosubstrate, at pH 7.6 and 25°C
0.036
fumarate
-
with reduced methyl viologen as cosubstrate, at pH 7.0 and 25°C
0.043
fumarate
wild type enzyme, with reduced methyl viologen as cosubstrate, at pH 6.0 and 25°C
0.043
fumarate
-
with reduced methyl viologen as cosubstrate, at pH 6.0 and 25°C
0.2
succinate
-
with oxidized 2,6-dichlorophenolindophenol as cosubstrate, at pH 7.4, temperature not specified in the publication
0.6
succinate
-
with oxidized 2,6-dichlorophenolindophenol as cosubstrate, at pH 8.8 and 25°C
0.8
succinate
-
with oxidized 2,6-dichlorophenolindophenol as cosubstrate, at pH 8.5 and 25°C
1.1
succinate
-
with oxidized 2,6-dichlorophenolindophenol as cosubstrate, at pH 9.0 and 25°C
2.2
succinate
-
with oxidized 2,6-dichlorophenolindophenol as cosubstrate, at pH 8.0 and 25°C
2.5
succinate
-
with oxidized 2,6-dichlorophenolindophenol as cosubstrate, at pH 9.5 and 25°C
2.6
succinate
-
with oxidized 2,6-dichlorophenolindophenol as cosubstrate, at pH 10.0 and 25°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
15
fumarate
mutant enzyme H61M, with reduced methyl viologen as cosubstrate, at pH 9.0 and 25°C
29
fumarate
mutant enzyme H61A, with reduced methyl viologen as cosubstrate, at pH 9.0 and 25°C
47
fumarate
mutant enzyme H61A, with reduced methyl viologen as cosubstrate, at pH 7.5 and 25°C
49
fumarate
mutant enzyme H61A, with reduced methyl viologen as cosubstrate, at pH 7.2 and 25°C
96
fumarate
mutant enzyme H61M, with reduced methyl viologen as cosubstrate, at pH 7.5 and 25°C
98
fumarate
mutant enzyme H61M, with reduced methyl viologen as cosubstrate, at pH 6.0 and 25°C
100
fumarate
mutant enzyme H61M, with reduced methyl viologen as cosubstrate, at pH 7.2 and 25°C
116
fumarate
mutant enzyme H61A, with reduced methyl viologen as cosubstrate, at pH 6.0 and 25°C
210
fumarate
wild type enzyme, with reduced methyl viologen as cosubstrate, at pH 9.0 and 25°C
250
fumarate
-
with reduced methyl viologen as cosubstrate, at pH 7.4, temperature not specified in the publication
345
fumarate
-
with reduced methyl viologen as cosubstrate, at pH 8.0 and 25°C
370
fumarate
wild type enzyme, with reduced methyl viologen as cosubstrate, at pH 7.5 and 25°C
409
fumarate
-
with reduced methyl viologen as cosubstrate, at pH 7.6 and 25°C
509
fumarate
wild type enzyme, with reduced methyl viologen as cosubstrate, at pH 7.2 and 25°C
509
fumarate
-
with reduced methyl viologen as cosubstrate, at pH 7.2 and 25°C
587
fumarate
-
with reduced methyl viologen as cosubstrate, at pH 7.0 and 25°C
658
fumarate
wild type enzyme, with reduced methyl viologen as cosubstrate, at pH 6.0 and 25°C
658
fumarate
-
with reduced methyl viologen as cosubstrate, at pH 6.0 and 25°C
0.07
succinate
-
with oxidized 2,6-dichlorophenolindophenol as cosubstrate, at pH 7.4, temperature not specified in the publication
0.4
succinate
-
with oxidized 2,6-dichlorophenolindophenol as cosubstrate, at pH 8.8 and 25°C
0.6
succinate
-
with oxidized 2,6-dichlorophenolindophenol as cosubstrate, at pH 8.0 and 25°C
0.7
succinate
-
with oxidized 2,6-dichlorophenolindophenol as cosubstrate, at pH 8.5 and 25°C
0.73
succinate
-
with oxidized 2,6-dichlorophenolindophenol as cosubstrate, at pH 9.0 and 25°C
0.95
succinate
-
with oxidized 2,6-dichlorophenolindophenol as cosubstrate, at pH 10.0 and 25°C
1.36
succinate
-
with oxidized 2,6-dichlorophenolindophenol as cosubstrate, at pH 9.5 and 25°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
14000
fumarate
-
with reduced methyl viologen as cosubstrate, at pH 7.6 and 25°C
15000
fumarate
-
with reduced methyl viologen as cosubstrate, at pH 6.0 and 25°C
16000
fumarate
-
with reduced methyl viologen as cosubstrate, at pH 7.0 and 25°C
19000
fumarate
-
with reduced methyl viologen as cosubstrate, at pH 8.0 and 25°C
21000
fumarate
-
with reduced methyl viologen as cosubstrate, at pH 7.2 and 25°C
0.272
succinate
-
with oxidized 2,6-dichlorophenolindophenol as cosubstrate, at pH 8.0 and 25°C
0.362
succinate
-
with oxidized 2,6-dichlorophenolindophenol as cosubstrate, at pH 10.0 and 25°C
0.544
succinate
-
with oxidized 2,6-dichlorophenolindophenol as cosubstrate, at pH 9.5 and 25°C
0.675
succinate
-
with oxidized 2,6-dichlorophenolindophenol as cosubstrate, at pH 9.0 and 25°C
0.727
succinate
-
with oxidized 2,6-dichlorophenolindophenol as cosubstrate, at pH 8.8 and 25°C
0.933
succinate
-
with oxidized 2,6-dichlorophenolindophenol as cosubstrate, at pH 8.5 and 25°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.002
mesaconic acid
-
at pH 7.4, temperature not specified in the publication
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Shewanella putrefaciens NCMB 400
formerly named Shewanella putrefaciens
UniProt
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
-
FccA is the key enzyme for fumarate reduction in Shewanella oneidensis MR-1. The enzyme is also used to remove the selenite already entered into the periplastic space
physiological function
malfunction
disruption of the enzyme gene leads to a specific loss of the ability to grow with fumarate as terminal electron acceptor
malfunction
Shewanella putrefaciens NCIMB 400
-
disruption of the enzyme gene leads to a specific loss of the ability to grow with fumarate as terminal electron acceptor
-
physiological function
the enzyme is essential for fumarate respiration
physiological function
-
the enzyme is a transient electron storage protein and could function in both the electron transport to fumarate and via MtrA to mineral-phase Fe(III)
physiological function
the protein is involved in the respiration of iron
physiological function
-
the protein is involved in the respiration of iron
-
physiological function
Shewanella putrefaciens NCIMB 400
-
the enzyme is essential for fumarate respiration
-
Show AA Sequence and Transmembrane Helices (113 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 100 mM Tris-HCl buffer (pH 7.8-8.5), 80 mM NaCl, 16-19% (w/v) PEG 8000, and 10 mM fumarate
hanging drop vapor diffusion method, using 100 mM Tris-HCl, pH 7.4, 80 mM NaCl, 17-20% (w/v) PEG 8000, and 10 mM fumarate
hanging drop vapor diffusion method, using 12% (w/v) PEG 20K and 100 mM Na MES pH 6.5
hanging drop vapor diffusion method, using 50-100 mM Tris-HCl, pH 7.4. 80 mM NaCl, 17-20% (w/v) PEG 8000, 10 mM fumarate
mutant enzymes H61M and H61A, hanging drop vapor diffusion method, using 100 mM Tris-HCl buffer (pH 7.8-8.5), 80 mM NaCl, 16-19% (w/v) PEG 8000, and 10 mM fumarate
small tetraheme cytochrome c, hanging drop vapor diffusion method, using 3.5-3.8 M ammonium sulfate, 0.1 M Bicine (pH 8.5-9.2)
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H365A
H365A/H504A
the mutant shows still some residual activity. The double mutation has a large effect on the Km value for fumarate, with the value in the millimolar range, and the effect on kcat is also dramatic
H504A
H61A
H61M
the mutant is catalytically active but exhibits marked decrease (5fold) in the value of kcat for fumarate reduction with respect to that of the wild type enzyme. The fumarate reductase activity of the mutant enzyme can be recovered to around 80% of that seen for the wild type by the addition of exogenous imidazole
Q363F
the mutant enzyme shows a water molecule which can account for its measured fumarate reductase activity. Values of kcat are about 1000fold lower than in the wild type enzyme, but with hugely elevated KM values in the millimolar region
Q363F/R402A
the elimination of fumarate reductase activity by mutation R402A is partially reversed by the additional substitution of Gln363 with phenylalanine. The mutation introduces a water molecule at the correct position in the active site to allow it to act as the catalytic proton donor. The Km values for the mutant are about 5fold lower than those of the wild type enzyme, decreasing slightly with increasing pH
R402A
R402K
-
the mutant exhibits activity, albeit at an extremely low level as compared to the wild type enzyme
H365A
-
the mutant enzyme exhibits lower kcat values than the wild type enzyme by factors of 3-15, depending on pH. This is coupled with the increase in Km
-
H504A
-
the mutant enzyme exhibits lower kcat values than the wild type enzyme by factors of 3-15, depending on pH. This is coupled with the increase in Km
-
R402A
-
the mutation leads to a dramatic loss of activity compared to the wild type enzyme
-
R402K
-
the mutant exhibits activity, albeit at an extremely low level as compared to the wild type enzyme
-
H365A
the mutant enzyme exhibits lower kcat values than the wild type enzyme by factors of 3-15, depending on pH. This is coupled with the increase in Km values
H365A
-
the mutant enzyme exhibits lower kcat values than the wild type enzyme by factors of 3-15, depending on pH. This is coupled with the increase in Km
H504A
the mutant enzyme exhibits lower kcat values than the wild type enzyme by factors of 3-15, depending on pH. This is coupled with the increase in Km values
H504A
-
the mutant enzyme exhibits lower kcat values than the wild type enzyme by factors of 3-15, depending on pH. This is coupled with the increase in Km
H61A
the mutant is catalytically active but exhibits marked decrease (10fold) in the value of kcat for fumarate reduction with respect to that of the wild type enzyme. The fumarate reductase activity of the mutant enzyme can be recovered to around 80% of that seen for the wild type by the addition of exogenous imidazole
H61A
-
in the mutated enzyme, heme IV is a five-coordinated high spin haem and so the NMR signals of the heme substituents are shifted to low field
R402A
the mutant enzyme has no detectable fumarate reductase activity
R402A
-
the mutation leads to a dramatic loss of activity compared to the wild type enzyme
R402A
the mutation eliminates the fumarate reductase activity of the enzyme
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, DEAE-Sepharose column chromatography and hydroxyapatite column chromatography
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in the DELTAfccA Shewanella frigidimarina strain EG301
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme expression is induced during anaerobic growth in the presence of 50 mM FeIII citrate
enzyme expression is regulated by anaerobiosis and by the availability of alternative electron acceptors, particularly nitrate and trimethylamine N-oxide
the enzyme expression is clearly induced by anaerobiosis and by the presence of fumarate in the growth medium
the enzyme is induced by Fe3+
enzyme expression is induced during anaerobic growth in the presence of 50 mM FeIII citrate
enzyme expression is induced during anaerobic growth in the presence of 50 mM FeIII citrate
-
-
enzyme expression is regulated by anaerobiosis and by the availability of alternative electron acceptors, particularly nitrate and trimethylamine N-oxide
enzyme expression is regulated by anaerobiosis and by the availability of alternative electron acceptors, particularly nitrate and trimethylamine N-oxide
Shewanella putrefaciens NCIMB 400
-
-
the enzyme expression is clearly induced by anaerobiosis and by the presence of fumarate in the growth medium
-
the enzyme expression is clearly induced by anaerobiosis and by the presence of fumarate in the growth medium
Shewanella putrefaciens NCMB 400
-
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Rothery, E.L.; Mowat, C.G.; Miles, C.S.; Walkinshaw, M.D.; Reid, G.A.; Chapman, S.K.
Histidine 61: an important heme ligand in the soluble fumarate reductase from Shewanella frigidimarina
Biochemistry
42
13160-13169
2003
Shewanella frigidimarina (P0C278)
brenda
Pessanha, M.; Rothery, E.L.; Miles, C.S.; Reid, G.A.; Chapman, S.K.; Louro, R.O.; Turner, D.L.; Salgueiro, C.A.; Xavier, A.V.
Tuning of functional heme reduction potentials in Shewanella fumarate reductases
Biochim. Biophys. Acta
1787
113-120
2009
Shewanella frigidimarina, Shewanella frigidimarina NCIMB400, Shewanella oneidensis
brenda
Bamford, V.; Dobbin, P.S.; Lee, S.C.; Reilly, A.; Powell, A.K.; Richardson, D.J.; Hemmings, A.M.
Crystallization and preliminary X-ray crystallographic analysis of a periplasmic tetrahaem flavocytochrome c3 from Shewanella frigidimarina NCIMB400 which has fumarate reductase activity
Acta Crystallogr. Sect. D
55
1222-1225
1999
Shewanella frigidimarina (Q9Z4P0), Shewanella frigidimarina NCIMB 400 (Q9Z4P0)
brenda
Schuetz, B.; Schicklberger, M.; Kuermann, J.; Spormann, A.M.; Gescher, J.
Periplasmic electron transfer via the c-type cytochromes MtrA and FccA of Shewanella oneidensis MR-1
Appl. Environ. Microbiol.
75
7789-7796
2009
Shewanella oneidensis
brenda
Morris, C.J.; Black, A.C.; Pealing, S.L.; Manson, F.D.; Chapman, S.K.; Reid, G.A.; Gibson, D.M.; Ward, F.B.
Purification and properties of a novel cytochrome flavocytochrome c from Shewanella putrefaciens
Biochem. J.
302
587-593
1994
Shewanella putrefaciens, Shewanella putrefaciens NCMB 400
brenda
Pessanha, M.; Louro, R.O.; Correia, I.J.; Rothery, E.L.; Pankhurst, K.L.; Reid, G.A.; Chapman, S.K.; Turner, D.L.; Salgueiro, C.A.
Thermodynamic characterization of a tetrahaem cytochrome isolated from a facultative aerobic bacterium, Shewanella frigidimarina a putative redox model for flavocytochrome c3
Biochem. J.
370
489-495
2003
Shewanella frigidimarina (Q07WU7), Shewanella frigidimarina NCIMB 400 (Q07WU7)
brenda
Reid, G.; Gordon, E.; Hil, A.; Doherty, M.; Turner, K.; Holt, R.; Chapman, S.
Structure and function of flavocytochrome c3, the soluble fumarate reductase from Shewanella NCIMB400
Biochem. Soc. Trans.
26
418-421
1998
Shewanella putrefaciens (Q07WU7), Shewanella putrefaciens NCIMB400 (Q07WU7)
-
brenda
Schwalb, C.; Chapman, S.K.; Reid, G.A.
The membrane-bound tetrahaem c-type cytochrome CymA interacts directly with the soluble fumarate reductase in Shewanella
Biochem. Soc. Trans.
30
658-662
2002
Shewanella oneidensis
brenda
Pealing, S.L.; Black, A.C.; Manson, F.D.; Ward, F.B.; Chapman, S.K.; Reid, G.A.
Sequence of the gene encoding flavocytochrome c from Shewanella putrefaciens a tetraheme flavoenzyme that is a soluble fumarate reductase related to the membrane-bound enzymes from other bacteria
Biochemistry
31
12132-12140
1992
Shewanella putrefaciens, Shewanella putrefaciens NCMB 400
brenda
Turner, K.L.; Doherty, M.K.; Heering, H.A.; Armstrong, F.A.; Reid, G.A.; Chapman, S.K.
Redox properties of flavocytochrome c3 from Shewanella frigidimarina NCIMB400
Biochemistry
38
3302-3309
1999
Shewanella frigidimarina, Shewanella frigidimarina NCIMB400
brenda
Doherty, M.; Pealing, S.; Miles, C.; Moysey, R.; Taylor, P.; Walkinshaw, M.; Reid, G.; Chapman, S.
Identification of the active site acid/base catalyst in a bacterial fumarate reductase A kinetic and crystallographic study
Biochemistry
39
10695-10701
2000
Shewanella frigidimarina (P0C278)
brenda
Mowat, C.G.; Pankhurst, K.L.; Miles, C.S.; Leys, D.; Walkinshaw, M.D.; Reid, G.A.; Chapman, S.K.
Engineering water to act as an active site acid catalyst in a soluble fumarate reductase
Biochemistry
41
11990-11996
2002
Shewanella frigidimarina (P0C278)
brenda
Reid, G.A.; Miles, C.S.; Moysey, R.K.; Pankhurst, K.L.; Chapman, S.K.
Catalysis in fumarate reductase
Biochim. Biophys. Acta
1459
310-315
2000
Shewanella frigidimarina, Shewanella frigidimarina NCIMB400
brenda
Paquete, C.M.; Saraiva, I.H.; Louro, R.O.
Redox tuning of the catalytic activity of soluble fumarate reductases from Shewanella
Biochim. Biophys. Acta
1837
717-725
2014
Shewanella frigidimarina, Shewanella frigidimarina NCIMB400, Shewanella oneidensis
brenda
Pessanha, M.; Rothery, E.L.; Louro, R.O.; Turner, D.L.; Miles, C.S.; Reid, G.A.; Chapman, S.K.; Xavier, A.V.; Salgueiro, C.A.
Redox behaviour of the haem domain of flavocytochrome c3 from Shewanella frigidimarina probed by NMR
FEBS Lett.
578
185-190
2004
Shewanella frigidimarina
brenda
Maier, T.M.; Myers, J.M.; Myers, C.R.
Identification of the gene encoding the sole physiological fumarate reductase in Shewanella oneidensis MR-1
J. Basic Microbiol.
43
312-327
2003
Shewanella oneidensis
brenda
Leys, D.; Meyer, T.E.; Tsapin, A.S.; Nealson, K.H.; Cusanovich, M.A.; Van Beeumen, J.J.
Crystal structures at atomic resolution reveal the novel concept of electron-harvesting as a role for the small tetraheme cytochrome c
J. Biol. Chem.
277
35703-35711
2002
Shewanella oneidensis (Q8EDL6)
brenda
Pealing, S.L.; Lysek, D.A.; Taylor, P.; Alexeev, D.; Reid, G.A.; Chapman, S.K.; Walkinshaw, M.D.
Crystallization and preliminary X-ray analysis of flavocytochrome c3, the fumarate reductase from Shewanella frigidimarina
J. Struct. Biol.
127
76-78
1999
Shewanella frigidimarina (P0C278), Shewanella frigidimarina ACAM591 (P0C278), Shewanella frigidimarina NCIMB 400 (P0C278)
brenda
Gordon, E.H.J.; Pealing, S.L.; Chapman, S.K.; Ward, F.B.; Reid, G.A.
Physiological function and regulation of flavocytochrome c3, the soluble fumarate reductase from Shewanella putrefaciens NCIMB 400
Microbiology
144
937-945
1998
Shewanella putrefaciens (Q9Z4P0), Shewanella putrefaciens NCIMB 400 (Q9Z4P0)
brenda
Bamford, V.; Dobbin, P.S.; Richardson, D.J.; Hemmings, A.M.
Open conformation of a flavocytochrome c3 fumarate reductase
Nat. Struct. Biol.
6
1104-1107
1999
Shewanella frigidimarina (Q9Z4P0), Shewanella frigidimarina NCIMB 400 (Q9Z4P0)
brenda
Taylor, P.; Pealing, S.L.; Reid, G.A.; Chapman, S.K.; Walkinshaw, M.D.
Structural and mechanistic mapping of a unique fumarate reductase
Nat. Struct. Biol.
6
1108-1112
1999
Shewanella frigidimarina (P0C278), Shewanella frigidimarina NCIMB 400 (P0C278)
brenda
Li, D.B.; Cheng, Y.Y.; Wu, C.; Li, W.W.; Li, N.; Yang, Z.C.; Tong, Z.H.; Yu, H.Q.
Selenite reduction by Shewanella oneidensis MR-1 is mediated by fumarate reductase in periplasm
Sci. Rep.
4
3735
2014
Shewanella oneidensis
brenda
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