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Information on EC 7.1.1.1 - proton-translocating NAD(P)+ transhydrogenase
for references in articles please use BRENDA:EC7.1.1.1
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EC Tree 7 Translocases
7.1 Catalysing the translocation of hydrons
7.1.1 Linked to oxidoreductase reactions
7.1.1.1 proton-translocating NAD(P)+ transhydrogenase
IUBMB Comments
The enzyme is a membrane bound proton-translocating pyridine nucleotide transhydrogenase that couples the reversible reduction of NADP by NADH to an inward proton translocation across the membrane. In the bacterium Escherichia coli the enzyme provides a major source of cytosolic NADPH. Detoxification of reactive oxygen species in mitochondria by glutathione peroxidases depends on NADPH produced by this enzyme.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
- 7.1.1.1
- nadp+
-
nadph-binding
- 3-acetylpyridine-nad+
- thio-nadp+
-
proteoliposomes
-
hydride
-
cysteine-free
-
membrane-spanning
-
dissipation
-
protrude
-
alpha-helices
-
detergent-dispersed
-
microbalance
- quartz
-
unspecific
-
palmitoyl-coenzyme
showSynonyms
proton-pumping nicotinamide nucleotide transhydrogenase, proton-translocating nad(p)+ transhydrogenase, proton translocating nicotinamide nucleotide transhydrogenase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EC 1.6.1.5
-
-
formerly
-
nicotinamide nucleotide transhydrogenase
NNT
pntA
pntB
proton-translocating NAD(P)(+) transhydrogenase
proton-translocating nicotinamide nucleotide transhydrogenase
-
-
proton-translocating transhydrogenase
pyridine nucleotide transhydrogenase
transhydrogenase
TT_C1779
NNT
-
-
-
-
pntA
-
-
-
-
pntB
-
-
-
-
proton-translocating transhydrogenase
-
-
proton-translocating transhydrogenase
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
NADPH + NAD+ + H+[side 1] = NADP+ + NADH + H+[side 2]
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
NAD phosphorylation and dephosphorylation, NAD phosphorylation and transhydrogenation
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SYSTEMATIC NAME
IUBMB Comments
NADPH:NAD+ oxidoreductase (H+-transporting)
The enzyme is a membrane bound proton-translocating pyridine nucleotide transhydrogenase that couples the reversible reduction of NADP by NADH to an inward proton translocation across the membrane. In the bacterium Escherichia coli the enzyme provides a major source of cytosolic NADPH. Detoxification of reactive oxygen species in mitochondria by glutathione peroxidases depends on NADPH produced by this enzyme.
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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
1,N6-etheno-NADPH + NAD+ + H+[side 1]
1,N6-etheno-NADP+ + NADH + H+[side 2]
-
Substrates: -
Products: -
Products: -
r
1,N6-etheno-NADPH + oxidized acetyl pyridine adenine dinucleotide + H+[side 1]
1,N6-etheno-NADP+ + reduced acetyl pyridine adenine dinucleotide + H+[side 2]
-
Substrates: -
Products: -
Products: -
r
deamino-NADPH + NAD+ + H+[side 1]
deamino-NADP+ + NADH + H+[side 2]
-
Substrates: -
Products: -
Products: -
r
deamino-NADPH + oxidized acetyl pyridine adenine dinucleotide + H+[side 1]
deamino-NADP+ + reduced acetyl pyridine adenine dinucleotide + H+[side 2]
-
Substrates: -
Products: -
Products: -
r
NADPH + 3-acetylpyridine-NAD+ + H+[side 1]
NADP+ + 3-acetylpyridine-NADH + H+[side 2]
-
Substrates: -
Products: -
Products: -
?
NADPH + NAD+ + H+/in
NADP+ + NADH + H+/out
-
Substrates: -
Products: -
Products: -
r
NADPH + oxidized 3-acetylpyridin-adenine dinucleotide + H+[side 1]
NADP+ + reduced 3-acetylpyridin-adenine dinucleotide + H+[side 2]
NADPH + oxidized 3-acetylpyridine adenine dinucleotide
NADP+ + reduced 3-acetylpyridine adenine dinucleotide
-
Substrates: -
Products: -
Products: -
?
NADPH + oxidized 3-acetylpyridine adenine dinucleotide + H+ [side 1]
NADP+ + reduced 3-acetylpyridine adenine dinucleotide + H+[side 2]
-
Substrates: -
Products: -
Products: -
?
NADPH + oxidized 3-acetylpyridine adenine dinucleotide + H+[side 1]
NADP+ + reduced 3-acetylpyridine adenine dinucleotide + H+[side 2]
-
Substrates: -
Products: -
Products: -
r
NADPH + oxidized acetyl pyridine adenine dinucleotide + H+/in
NADP+ + reduced acetyl pyridine adenine dinucleotide + H+/out
-
Substrates: -
Products: -
Products: -
r
NADPH + oxidized acetyl pyridine adenine dinucleotide + H+[side 1]
NADP+ + reduced acetyl pyridine adenine dinucleotide + H+[side 2]
NADPH + oxidized acetylpyridine adenine dinucleotide + H+[side 1]
NADP+ + reduced acetylpyridine adenine dinucleotide + H+[side 2]
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: NADP(H) binding leads to perturbation of a deeply buried part of the polypeptide backbone and to protonation of a carboxylic acid residue
Products: -
Products: -
?
H+(in) + NAD+ + NADPH
H+(out) + NADH + NADP+
Substrates: -
Products: -
Products: -
?
H+(in) + NAD+ + NADPH
H+(out) + NADH + NADP+
Substrates: -
Products: -
Products: -
?
H+/out + NADH + NADP+
H+/in + NAD+ + NADPH
Substrates: the enzyme couples the redox reaction between NAD(H) and NADP(H) to the inward transport of protons across a membrane
Products: -
Products: -
?
H+/out + NADH + NADP+
H+/in + NAD+ + NADPH
-
Substrates: the enzyme couples the redox reaction between NAD(H) and NADP(H) to the transport of protons across a membrane
Products: -
Products: -
?
NADH + NADP+
NAD+ + NADPH
-
Substrates: -
Products: -
Products: -
r
NADH + NADP+
NAD+ + NADPH
-
Substrates: reaction is catalyzed by a mixture of recombinant domains dI and dIII of either species or by a hybrid mixture of domains I and III from both species
Products: -
Products: -
?
NADH + NADP+
NAD+ + NADPH
-
Substrates: links hydride transfer between NAD(H) and NADP(H) to the outside in translocation of protons across membrane
Products: -
Products: -
r
NADH + NADP+
NAD+ + NADPH
-
Substrates: links hydride transfer between NAD(H) and NADP(H) to the translocation of protons across membrane
Products: -
Products: -
r
NADH + NADP+
NAD+ + NADPH
-
Substrates: links hydride transfer between NAD(H) and NADP(H) to the translocation of protons across membrane, cellular regeneration of NADPH
Products: -
Products: -
r
NADH + NADP+
NAD+ + NADPH
-
Substrates: links hydride transfer between NAD(H) and NADP(H) to the translocation of protons across membrane, major source of NADPH
Products: -
Products: -
r
NADH + NADP+
NAD+ + NADPH
-
Substrates: links hydride transfer between NAD(H) and NADP(H) to the translocation of protons across membrane, provides NADPH for biosynthesis and reduction of glutathione
Products: -
Products: -
r
NADH + NADP+
NAD+ + NADPH
-
Substrates: links hydride transfer between NAD(H) and NADP(H) to the translocation of protons across membrane, provides NADPH for the reduction of glutathione, reverse reaction results in outward proton translocation and creation of a proton motive force
Products: -
Products: -
r
NADH + NADP+
NAD+ + NADPH
Substrates: links hydride transfer between NAD(H) and NADP(H) to the translocation of protons across membrane, provides NADPH for biosynthesis and glutathione reduction
Products: -
Products: -
r
NADH + NADP+
NAD+ + NADPH
-
Substrates: solubilized and purified enzyme does not catalyze reduction of acetyl pyridine adenine dinucleotide by NADH in absence of NADP+
Products: -
Products: -
?
NADH + NADP+
NAD+ + NADPH
-
Substrates: reaction is catalyzed by a mixture of recombinant domains dI and dIII of either species or by a hybrid mixture of domains I and III from both species
Products: -
Products: -
?
NADH + NADP+
NAD+ + NADPH
-
Substrates: links hydride transfer between NAD(H) and NADP(H) to the outside in translocation of protons across membrane, provides NADPH for biosynthesis and reduction of glutathione, reaction is stereospecific between th 4A position of NAD(H) to the 4B position of NADP(H)
Products: -
Products: -
r
NADH + NADP+
NAD+ + NADPH
-
Substrates: links hydride transfer between NAD(H) and NADP(H) to the translocation of protons across membrane
Products: -
Products: -
r
NADH + NADP+
NAD+ + NADPH
Substrates: links hydride transfer between NAD(H) and NADP(H) to the translocation of protons across membrane, provides NADPH for biosynthesis and glutathione reduction
Products: -
Products: -
r
NADH + NADP+
NAD+ + NADPH
-
Substrates: links hydride transfer between NAD(H) and NADP(H) to the translocation of protons across membrane, provides NADPH for biosynthesis and reduction of glutathione
Products: -
Products: -
r
NADP+ + NADH
NADPH + NAD+
-
Substrates: mitochondrial transhydrogenase is stereospecific for the 4A-NADH and 4B-NADPH hydrogens
Products: -
Products: -
?
NADP+ + NADH
NADPH + NAD+
-
Substrates: mitochondrial transhydrogenase is stereospecific for the 4A-NADH and 4B-NADPH hydrogens
Products: -
Products: -
?
NADPH + 3-acetylpyridine-NAD+
3-acetylpyridine-NADH + NADP+
-
Substrates: -
Products: -
Products: -
?
NADPH + 3-acetylpyridine-NAD+
3-acetylpyridine-NADH + NADP+
-
Substrates: -
Products: -
Products: -
?
NADPH + NAD+ + H+[side 1]
NADP+ + NADH + H+[side 2]
-
Substrates: -
Products: -
Products: -
?
NADPH + NAD+ + H+[side 1]
NADP+ + NADH + H+[side 2]
-
Substrates: -
Products: -
Products: -
r
NADPH + NAD+ + H+[side 1]
NADP+ + NADH + H+[side 2]
Substrates: -
Products: -
Products: -
?
NADPH + NAD+ + H+[side 1]
NADP+ + NADH + H+[side 2]
-
Substrates: -
Products: -
Products: -
r
NADPH + NAD+ + H+[side 1]
NADP+ + NADH + H+[side 2]
-
Substrates: -
Products: -
Products: -
r
NADPH + NAD+ + H+[side 1]
NADP+ + NADH + H+[side 2]
-
Substrates: -
Products: -
Products: -
r
NADPH + NAD+ + H+[side 1]
NADP+ + NADH + H+[side 2]
-
Substrates: -
Products: -
Products: -
?
NADPH + NAD+ + H+[side 1]
NADP+ + NADH + H+[side 2]
-
Substrates: -
Products: -
Products: -
?
NADPH + NAD+ + H+[side 1]
NADP+ + NADH + H+[side 2]
Substrates: -
Products: -
Products: -
?
NADPH + NAD+ + H+[side 1]
NADP+ + NADH + H+[side 2]
-
Substrates: -
Products: -
Products: -
?
NADPH + NAD+ + H+[side 1]
NADP+ + NADH + H+[side 2]
-
Substrates: -
Products: -
Products: -
r
NADPH + NAD+ + H+[side 1]
NADP+ + NADH + H+[side 2]
-
Substrates: -
Products: -
Products: -
?
NADPH + NAD+ + H+[side 1]
NADP+ + NADH + H+[side 2]
Substrates: -
Products: -
Products: -
?
NADPH + NAD+ + H+[side 1]
NADP+ + NADH + H+[side 2]
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
Substrates: -
Products: -
Products: -
?
NADPH + oxidized 3-acetylpyridin-adenine dinucleotide + H+[side 1]
NADP+ + reduced 3-acetylpyridin-adenine dinucleotide + H+[side 2]
-
Substrates: -
Products: -
Products: -
?
NADPH + oxidized 3-acetylpyridin-adenine dinucleotide + H+[side 1]
NADP+ + reduced 3-acetylpyridin-adenine dinucleotide + H+[side 2]
-
Substrates: -
Products: -
Products: -
?
NADPH + oxidized acetyl pyridine adenine dinucleotide + H+[side 1]
NADP+ + reduced acetyl pyridine adenine dinucleotide + H+[side 2]
-
Substrates: -
Products: -
Products: -
?
NADPH + oxidized acetyl pyridine adenine dinucleotide + H+[side 1]
NADP+ + reduced acetyl pyridine adenine dinucleotide + H+[side 2]
-
Substrates: -
Products: -
Products: -
r
NADPH + oxidized acetyl pyridine adenine dinucleotide + H+[side 1]
NADP+ + reduced acetyl pyridine adenine dinucleotide + H+[side 2]
Substrates: -
Products: -
Products: -
r
NADPH + oxidized acetyl pyridine adenine dinucleotide + H+[side 1]
NADP+ + reduced acetyl pyridine adenine dinucleotide + H+[side 2]
-
Substrates: -
Products: -
Products: -
r
NADPH + oxidized acetyl pyridine adenine dinucleotide + H+[side 1]
NADP+ + reduced acetyl pyridine adenine dinucleotide + H+[side 2]
-
Substrates: -
Products: -
Products: -
r
NADPH + oxidized acetyl pyridine adenine dinucleotide + H+[side 1]
NADP+ + reduced acetyl pyridine adenine dinucleotide + H+[side 2]
-
Substrates: -
Products: -
Products: -
r
NADPH + oxidized acetyl pyridine adenine dinucleotide + H+[side 1]
NADP+ + reduced acetyl pyridine adenine dinucleotide + H+[side 2]
-
Substrates: -
Products: -
Products: -
?
NADPH + oxidized acetyl pyridine adenine dinucleotide + H+[side 1]
NADP+ + reduced acetyl pyridine adenine dinucleotide + H+[side 2]
-
Substrates: -
Products: -
Products: -
r
thio-NADP+ + NADH + H+[side 2]
thio-NADPH + NAD+ + H+[side 1]
-
Substrates: -
Products: -
Products: -
?
thio-NADP+ + NADH + H+[side 2]
thio-NADPH + NAD+ + H+[side 1]
-
Substrates: -
Products: -
Products: -
r
thio-NADPH + NAD+ + H+[side 1]
thio-NADP+ + NADH + H+[side 2]
-
Substrates: -
Products: -
Products: -
?
thio-NADPH + NAD+ + H+[side 1]
thio-NADP+ + NADH + H+[side 2]
-
Substrates: -
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
NADPH + NAD+ + H+/in
NADP+ + NADH + H+/out
-
Substrates: -
Products: -
Products: -
r
NADPH + oxidized 3-acetylpyridine adenine dinucleotide
NADP+ + reduced 3-acetylpyridine adenine dinucleotide
-
Substrates: -
Products: -
Products: -
?
H+/out + NADH + NADP+
H+/in + NAD+ + NADPH
Substrates: the enzyme couples the redox reaction between NAD(H) and NADP(H) to the inward transport of protons across a membrane
Products: -
Products: -
?
H+/out + NADH + NADP+
H+/in + NAD+ + NADPH
-
Substrates: the enzyme couples the redox reaction between NAD(H) and NADP(H) to the transport of protons across a membrane
Products: -
Products: -
?
NADH + NADP+
NAD+ + NADPH
-
Substrates: links hydride transfer between NAD(H) and NADP(H) to the outside in translocation of protons across membrane
Products: -
Products: -
r
NADH + NADP+
NAD+ + NADPH
-
Substrates: links hydride transfer between NAD(H) and NADP(H) to the translocation of protons across membrane
Products: -
Products: -
r
NADH + NADP+
NAD+ + NADPH
-
Substrates: links hydride transfer between NAD(H) and NADP(H) to the translocation of protons across membrane, cellular regeneration of NADPH
Products: -
Products: -
r
NADH + NADP+
NAD+ + NADPH
-
Substrates: links hydride transfer between NAD(H) and NADP(H) to the translocation of protons across membrane, major source of NADPH
Products: -
Products: -
r
NADH + NADP+
NAD+ + NADPH
-
Substrates: links hydride transfer between NAD(H) and NADP(H) to the translocation of protons across membrane, provides NADPH for biosynthesis and reduction of glutathione
Products: -
Products: -
r
NADH + NADP+
NAD+ + NADPH
-
Substrates: links hydride transfer between NAD(H) and NADP(H) to the translocation of protons across membrane, provides NADPH for the reduction of glutathione, reverse reaction results in outward proton translocation and creation of a proton motive force
Products: -
Products: -
r
NADH + NADP+
NAD+ + NADPH
Substrates: links hydride transfer between NAD(H) and NADP(H) to the translocation of protons across membrane, provides NADPH for biosynthesis and glutathione reduction
Products: -
Products: -
r
NADH + NADP+
NAD+ + NADPH
-
Substrates: links hydride transfer between NAD(H) and NADP(H) to the outside in translocation of protons across membrane, provides NADPH for biosynthesis and reduction of glutathione, reaction is stereospecific between th 4A position of NAD(H) to the 4B position of NADP(H)
Products: -
Products: -
r
NADH + NADP+
NAD+ + NADPH
-
Substrates: links hydride transfer between NAD(H) and NADP(H) to the translocation of protons across membrane
Products: -
Products: -
r
NADH + NADP+
NAD+ + NADPH
Substrates: links hydride transfer between NAD(H) and NADP(H) to the translocation of protons across membrane, provides NADPH for biosynthesis and glutathione reduction
Products: -
Products: -
r
NADH + NADP+
NAD+ + NADPH
-
Substrates: links hydride transfer between NAD(H) and NADP(H) to the translocation of protons across membrane, provides NADPH for biosynthesis and reduction of glutathione
Products: -
Products: -
r
NADPH + NAD+ + H+[side 1]
NADP+ + NADH + H+[side 2]
-
Substrates: -
Products: -
Products: -
?
NADPH + NAD+ + H+[side 1]
NADP+ + NADH + H+[side 2]
-
Substrates: -
Products: -
Products: -
r
NADPH + NAD+ + H+[side 1]
NADP+ + NADH + H+[side 2]
Substrates: -
Products: -
Products: -
?
NADPH + NAD+ + H+[side 1]
NADP+ + NADH + H+[side 2]
-
Substrates: -
Products: -
Products: -
r
NADPH + NAD+ + H+[side 1]
NADP+ + NADH + H+[side 2]
-
Substrates: -
Products: -
Products: -
r
NADPH + NAD+ + H+[side 1]
NADP+ + NADH + H+[side 2]
-
Substrates: -
Products: -
Products: -
r
NADPH + NAD+ + H+[side 1]
NADP+ + NADH + H+[side 2]
-
Substrates: -
Products: -
Products: -
?
NADPH + NAD+ + H+[side 1]
NADP+ + NADH + H+[side 2]
-
Substrates: -
Products: -
Products: -
?
NADPH + NAD+ + H+[side 1]
NADP+ + NADH + H+[side 2]
Substrates: -
Products: -
Products: -
?
NADPH + NAD+ + H+[side 1]
NADP+ + NADH + H+[side 2]
-
Substrates: -
Products: -
Products: -
?
NADPH + NAD+ + H+[side 1]
NADP+ + NADH + H+[side 2]
-
Substrates: -
Products: -
Products: -
r
NADPH + NAD+ + H+[side 1]
NADP+ + NADH + H+[side 2]
-
Substrates: -
Products: -
Products: -
?
NADPH + NAD+ + H+[side 1]
NADP+ + NADH + H+[side 2]
Substrates: -
Products: -
Products: -
?
NADPH + NAD+ + H+[side 1]
NADP+ + NADH + H+[side 2]
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
no flavin cofactor, differentiation from EC 1.6.1.1.
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
K+
Mg2+
Na+
-
strong activation of forward reaction, i.e. the reduction of NADP+ by NADH, in the light at concentrations of approx. 50-80 mM, half-maximal activation at 10 mM
Ca2+
-
strong activation of forward reaction in the light at concentrations above 0.1 mM
K+
-
strong activation of forward reaction, i.e. the reduction of NADP+ by NADH, in the light at concentrations of approx. 50-80 mM, half-maximal activation at 10 mM
Mg2+
-
strong activation of forward reaction, i.e. the reduction of NADP+ by NADH, in the light at concentrations above 0.1 mM
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-(4-maleimidoanilino)-naphthalene-6-sulfonic acid
-
0.004 mM, 2 h incubation, 75% inhibition of reverse reaction catalyzed by A348C mutant enzyme, 95% inhibition of A390C mutant enzyme after 1 h, 90% inhibition of K424C mutant enzyme after 1 h, 55% inhibition of R425C mutant enzyme after 1h
Butane-2,3-dione
-
40 mM, almost complete inactivation of enzyme activity in chromatophores after 12 min, NAD+ and NADP+ partially protect, complete protection by a combination of NAD+ and NADP+
Cd2+
-
low concentrations of Cd2+ strongly inhibit revers transhydrogenation
N,N'-Dicylclohexylcarbodiimide
-
NADH protects from inhibition, NADP+ and to a lesser extent NADPH increase the rate of inhibition
N-cyclohexyl-N'-(4-dimethylaminonaphthyl)carbodiimide
-
about 25% residual activity after 200 min at 0.5 mM
NADP+
-
mixed product inhibition vs. acetylpyridine adenine dinucleotide, competitive vs. NADPH
oxidized 3-acetylpyridin-adenine dinucleotide
-
high concentrations of oxidized 3-acetylpyridin-adenine dinucleotide lead to substrate inhibition
reduced acetylpyridine adenine dinucleotide
-
competitive inhibition vs. oxidized acetylpyridine adenine dinucleotide, mixed inhibition vs. NADPH
Zn2+
-
low concentrations of Zn2+ strongly inhibit revers transhydrogenation
N,N'-dicyclohexylcarbodiimide
-
NADH protects the enzyme against inhibition by N,N'-dicyclohexylcarbodiimide, while NADP+ , and to a lesser extent NADPH increase the rate of inhibition
N,N'-dicyclohexylcarbodiimide
-
about 12% residual activity after 180 min at 0.5 mM
N,N'-dicyclohexylcarbodiimide
-
modification of the enzyme with N,N'-dicyclohexylcarbodiimide leads to inhibition of the rate of release of NADP+ and NADPH from the enzyme, but has a much smaller effect on the binding and release of NAD+, NADH and their analogues and on the interconversion of the ternary complexes of the enzyme with its substrates
N-ethylmaleimide
-
0.2 mM, 57% inhibition of reverse reaction in A348C mutant enzyme, 60% inhibition of K424C mutant enzyme, more than 95% inhibition of A390C mutant enzyme after 1h, R425C mutant enzyme is not inhibited
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
carbonylcyanide-4-trifluoromethoxyphenyl hydrazone
-
0.002 mM stimulates the rate of the forward reaction by 8fold and of the reverse reaction by 10fold
light
-
forward reaction in chromatophores is accelerated more than 20fold during illumination with photosynthetically active light
-
phosphatidylcholine
presence of phospholipid is required, most effective phopholipid tested
additional information
presence of phospholipid is required, without phospholipid activity is rapidly lost
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE