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Information on EC 1.18.1.2 - ferredoxin-NADP+ reductase and Organism(s) Bacillus subtilis and UniProt Accession O05268
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1.18.1.2 ferredoxin-NADP+ reductaseIUBMB Comments
A flavoprotein (FAD). In chloroplasts and cyanobacteria the enzyme acts on plant-type [2Fe-2S] ferredoxins, but in other bacteria it can also reduce bacterial [4Fe-4S] ferredoxins and flavodoxin.
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Word Map
- 1.18.1.2
- nitrate
- ferredoxins
-
denitrification
-
denitrify
- reductases
- heme
- fad
- spinach
- chloroplast
- copper
- ammonia
-
nitrous
- flavin
-
dissimilatory
- photosystems
- flavodoxins
- denitrificans
- alcaligenes
- paracoccus
- n2o
- anabaena
-
copper-containing
- thylakoids
-
anammox
- p450scc
- semiquinone
- diaphorase
- viologen
- azurins
-
ferredoxin-dependent
- stutzeri
-
plant-type
- achromobacter
-
flavoenzymes
-
electron-transfer
-
ammonia-oxidizing
- plastocyanin
-
dinitrogen
-
photoreduction
- gogat
- pregnenolone
-
nitrate-induced
- xylosoxidans
-
photoreduced
-
wolinella
- isoalloxazine
-
nitrate-reducing
- biotechnology
- nitrosomonas
-
deoxyhemoglobin
- agriculture
-
single-electron
The taxonomic range for the selected organisms is: Bacillus subtilis
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
nitrite reductase, adrenodoxin reductase, ferric reductase, ferredoxin-nadp+ reductase, ferredoxin-nadp reductase, ferredoxin-nadp(+) reductase, ferredoxin-nadp+ oxidoreductase, flavodoxin reductase, ferredoxin:nadp+ oxidoreductase, ferredoxin:nadp+ reductase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
adrenodoxin reductase
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-
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DA1
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ferredoxin-NADP oxidoreductase
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ferredoxin-NADP reductase
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-
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Ferredoxin-NADP(+) reductase
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ferredoxin-NADP-oxidoreductase
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-
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ferredoxin-nicotinamide-adenine dinucleotide phosphate (oxidized) reductase
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-
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ferredoxin-TPN reductase
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-
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ferredoxin:NADP+ oxidoreductase
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-
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Flavodoxin reductase
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-
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FLDR
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-
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FLXR
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-
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FNR
NADP:ferredoxin oxidoreductase
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NADPH:ferredoxin oxidoreductase
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-
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NFR
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-
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reduced nicotinamide adenine dinucleotide phosphate-adrenodoxin reductase
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-
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reductase, ferredoxin-nicotinamide adenine dinucleotide phosphate
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TPNH-ferredoxin reductase
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FNR
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-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH
a hydride transfer reaction with NAD(P)H and two separate one-electron transfer reactions with ferredoxin are generally involved in te reaction process
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
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-
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oxidation
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reduction
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SYSTEMATIC NAME
IUBMB Comments
ferredoxin:NADP+ oxidoreductase
A flavoprotein (FAD). In chloroplasts and cyanobacteria the enzyme acts on plant-type [2Fe-2S] ferredoxins, but in other bacteria it can also reduce bacterial [4Fe-4S] ferredoxins and flavodoxin.
CAS REGISTRY NUMBER
COMMENTARY
56367-57-8
-
9029-33-8
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2 oxidized ferredoxin + NADPH
2 reduced ferredoxin + NADP+ + H+
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-
-
r
NADH + 2 oxidized [2Fe-2S]-[ferredoxin]
H+ + NAD+ + 2 reduced [2Fe-2S]-[ferredoxin]
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-
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?
NADH + 2 oxidized [2Fe-2S]-[rubredoxin]
H+ + NAD+ + 2 reduced [2Fe-2S]-[rubredoxin]
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-
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?
NADPH + 2 oxidized [2Fe-2S]-[rubredoxin]
H+ + NADP+ + 2 reduced [2Fe-2S]-[rubredoxin]
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-
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?
NADPH + H+ + oxidized 2,6-dichlorophenolindophenol
NADP+ + reduced 2,6-dichlorophenolindophenol
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diaphorase activity, no activity with NADH
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-
?
reduced cytochrome c + NADP+
oxidized cytochrome c + NADPH + H+
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-
?
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH + H+
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-
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r
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH + H+
with K3[Fe(CN)6] as electron acceptor in the enzyme assay. Ferredoxin is a low-redox-potential iron-sulfur protein. BsFNR features two distinct binding domains for FAD and NADPH, the deduced mode of NADP+ binding to the BsFNR molecule is nonproductive in that the nicotinamide and isoalloxazine rings are over 15A A apart, binding structures, overview
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r
additional information
?
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enzyme catalyzes the reduction of rubredoxin at rates comparable to those reported for NADH-rubredoxin oxidoreductases. At high concentrations, substrate inhibition is observed with electron donor NADPH
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additional information
?
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enzyme catalyzes the reduction of rubredoxin at rates comparable to those reported for NADH-rubredoxin oxidoreductases. At high concentrations, substrate inhibition is observed with electron donor NADPH
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additional information
?
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the enzyme also shows NAD(P)H oxidase activity, overview
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?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2 oxidized ferredoxin + NADPH
2 reduced ferredoxin + NADP+ + H+
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-
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r
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH + H+
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r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
BsFNR features two distinct binding domains for FAD and NADPH, binding structure, overview. A unique C-terminal extension covers the re-face of the isoalloxazine moiety of FAD. Tyr50 in the FAD-binding region and His324 in the Cterminal extension stack on the si- and re-faces of the isoalloxazine ring of FAD, respectively
FAD
flavin adenine dinucleotide prosthetic group, the FAD prosthetic group is noncovalently bound in the open conformation. The fluorescence intensity of the protein-bound FAD is influenced by its environment. The fluorescence emissions of enzyme mutants Y50G and Y50S enzymes increase six to sevenfold compared with that of free FAD, whereas the fluorescence emission of wild-type and Y50W enzymes is efficiently quenched to below 3% and 9% of that of free FAD. ENzyme residue Tyr50 plays an important role to stabilize the FAD prosthetic group
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
rubredoxin
substrate inhibition is observed with electron donor NADPH
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.021
oxidized [2Fe-2S]-[rubredoxin]
cosubstrate NADPH, pH 7, 25°C
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additional information
additional information
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Michaelis-Menten kinetics
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additional information
additional information
Michaelis-Menten kinetics
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additional information
additional information
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below 0.1 mM, oxidized ferredoxin with NADH, pH 7.0, 24°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
enzyme catalyzes reactions of both EC 1.18.1.2 and EC 1.19.1.1
UniProt
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
FNR mediates the redox reaction between NADP+/NADPH and ferredoxin, providing redox equivalents in cell-material synthesis
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
additional information
additional information
structure, primary sequence and oligomeric conformation, comparisons, overview
additional information
-
structure, primary sequence and oligomeric conformation, comparisons, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
FNR in complex with NADP+, two different crystal forms, mixing of 0.001 ml of 10 mg/ml protein and 2.5 mM NADP+ with 0.001 ml of reservoir solution containing 0.1 M HEPES buffer, pH 7.5, 30% 1,2-propanediol, and 20% PEG 400 for form I, and 20% PEG 3350, 0.2 M sodium fluoride, and 5% trehalose for form II, 20°C, X-ray diffraction structure determination and analysis at 1.8-1.9 A resolution, respetively, molecular replacement
purified recombinant FNR in complex with NADP+ in two different forms, 0.001 ml of 10 mg/ml protein in 50 mM Tris-HCl pH 8.0, 200 mM NaCl, and 2.5 mM NADP+, is mixed with 0.001 ml reservoir solution, 20°C. The reservoir solutions consist of 0.1 M HEPES buffer pH 7.5, 30% 1,2-propanediol, 20% PEG 400 for form I, and of 20% PEG 3350, 0.2 M sodium fluoride and 5% trehalose for form II. X-ray diffraction structure determination and analysis at 1.8 and 1.9 A resolution, respectively, molecular replacement, modelling
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H324F
site-directed mutagenesis, the mutant shows altered kinetics and reduced activity compared to the wild-type FNR
H324S
site-directed mutagenesis, the mutant shows altered kinetics and reduced activity compared to the wild-type FNR
R186G
site-directed mutagenesis, replacement of Arg186 with glycine leads to drastically reduced amounts of recombinant protein
R186G/D187H
site-directed mutagenesis, the mutant shows altered kinetics and reduced activity compared to the wild-type FNR
R186G/D187H/R190Q
site-directed mutagenesis, the mutant shows altered kinetics and reduced activity compared to the wild-type FNR
R190Q
site-directed mutagenesis, the mutant shows altered kinetics and reduced activity compared to the wild-type FNR
Y50G
Y50S
Y50W
Y50G
the mutation decreases thermal stability compared to the wild type enzyme
Y50S
the mutation decreases thermal stability compared to the wild type enzyme
Y50W
the mutation decreases thermal stability compared to the wild type enzyme, The mutant retains approximately 20% of wild type reactivity
additional information
Y50G
mutation results in a blue shift of the FAD transition bands, with enhancement of fluorescence emission. Mutant displays decreased thermal stability
Y50G
site-directed mutagenesis, the mutant shows a blue shift of the FAD transition band and decreased thermal stability compared to wild-type. Using the diaphorase assay, the kcat values for the Y50G mutant in the presence of NADPH and ferricyanide is decreased to less than 5% of the wild-type activity
Y50S
mutation results in a blue shift of the FAD transition bands, with enhancement of fluorescence emission. Mutant displays decreased thermal stability
Y50S
site-directed mutagenesis, the mutant shows a blue shift of the FAD transition band and decreased thermal stability compared to wild-type. Using the diaphorase assay, the kcat values for the Y50G mutant in the presence of NADPH and ferricyanide is decreased to less than 5% of the wild-type activity
Y50W
mutation results in a blue shift of the FAD transition bands, with quenching of fluorescence emission. Mutant displays decreased thermal stability
Y50W
site-directed mutagenesis, the mutant shows a blue shift of the FAD transition band and decreased thermal stability compared to wild-type. The mutant retains approximately 20 % reactivity in the diaphorase assay and BsFd-dependent cytochrome c reduction assay relative to wild-type
additional information
site-directed mutagenesis of NADPH-specific BsFNR to replace Arg186, Asp187, Arg190, and His324 with the residues occurring in NADH/NADPH-bispecific Chlorobium tepidum FNR
additional information
-
site-directed mutagenesis of NADPH-specific BsFNR to replace Arg186, Asp187, Arg190, and His324 with the residues occurring in NADH/NADPH-bispecific Chlorobium tepidum FNR
additional information
-
replacement of Tyr50 stacked on the si-face of the isoalloxazine ring of the flavin adenine dinucleotide prosthetic group modulates Bacillus subtilis ferredoxin-NADP+ oxidoreductase activity toward NADPH. The Y50G and Y50S mutations enhance the FAD fluorescence emission, whereas those of the wild type and Y50W mutant are quenched
additional information
replacement of Tyr50 stacked on the si-face of the isoalloxazine ring of the flavin adenine dinucleotide prosthetic group modulates Bacillus subtilis ferredoxin-NADP+ oxidoreductase activity toward NADPH. The Y50G and Y50S mutations enhance the FAD fluorescence emission, whereas those of the wild type and Y50W mutant are quenched
additional information
-
the depletions of residues Y313 to K332 (whole C-terminal extension region) and S325 to K332 results in significant increases in the catalytic efficiency with NADPH in diaphorase assay with ferricyanide, whereas Km values for ferricyanide are increased. In the cytochrome c reduction assay in the presence of ferredoxin, the S325-K332 depleted mutant displays a significant decrease in the turnover rate. The Y313-K332 depleted mutant demonstrates an increase in the rate of the direct reduction of horse heart cytochrome c in the absence of ferredoxin
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme from cell extract 86fold to homogeneity by several chromatographic steps
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Seo, D.; Kamino, K.; Inoue, K.; Sakurai, H.
Purification and characterization of ferredoxin-NADP+ reductase encoded by Bacillus subtilis yumC
Arch. Microbiol.
182
80-89
2004
Bacillus subtilis
Komori, H.; Seo, D.; Sakurai, T.; Higuchi, Y.
Crystallization and preliminary X-ray studies of ferredoxin-NADP+ oxidoreductase encoded by Bacillus subtilis yumC
Acta Crystallogr. Sect. F
66
301-303
2010
Bacillus subtilis
Komori, H.; Seo, D.; Sakurai, T.; Higuchi, Y.
Crystal structure analysis of Bacillus subtilis ferredoxin-NADP+ oxidoreductase and the structural basis for its substrate selectivity
Protein Sci.
19
2279-2290
2010
Bacillus subtilis (O05268), Bacillus subtilis
Seo, D.; Naito, H.; Nishimura, E.; Sakurai, T.
Replacement of Tyr50 stacked on the si-face of the isoalloxazine ring of the flavin adenine dinucleotide prosthetic group modulates Bacillus subtilis ferredoxin-NADP+ oxidoreductase activity toward NADPH
Photosynth. Res.
125
321-328
2015
Bacillus subtilis (O05268), Bacillus subtilis 168 (O05268)
Seo, D.; Naito, H.; Nishimura, E.; Sakurai, T.
Replacement of Tyr50 stacked on the si-face of the isoalloxazine ring of the flavin adenine dinucleotide prosthetic group modulates Bacillus subtilis ferredoxin-NADP+ oxidoreductase activity toward NADPH
Photosynth. Res.
125
321-328
2015
Bacillus subtilis, Bacillus subtilis (O05268), Bacillus subtilis 168 (O05268)
Seo, D.; Asano, T.; Komori, H.; Sakurai, T.
Role of the C-terminal extension stacked on the re-face of the isoalloxazine ring moiety of the flavin adenine dinucleotide prosthetic group in ferredoxin-NADP+ oxidoreductase from Bacillus subtilis
Plant Physiol. Biochem.
81
143-148
2014
Bacillus subtilis, Bacillus subtilis 168
Ittarat, W.; Sato, T.; Kitashima, M.; Sakurai, H.; Inoue, K.; Seo, D.
Rubredoxin from the green sulfur bacterium Chlorobaculum tepidum donates a redox equivalent to the flavodiiron protein in an NAD(P)H dependent manner via ferredoxin-NAD(P)+ oxidoreductase
Arch. Microbiol.
203
799-808
2021
Bacillus subtilis (O05268), Bacillus subtilis, Chlorobaculum tepidum (Q8KCB2), Chlorobaculum tepidum, Bacillus subtilis 168 (O05268), Chlorobaculum tepidum DSM 12025 (Q8KCB2)
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