Information on EC 1.8.7.1 - assimilatory sulfite reductase (ferredoxin)

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The expected taxonomic range for this enzyme is: Eukaryota, Archaea, Bacteria

EC NUMBER
COMMENTARY hide
1.8.7.1
-
RECOMMENDED NAME
GeneOntology No.
assimilatory sulfite reductase (ferredoxin)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
hydrogen sulfide + 6 oxidized ferredoxin [iron-sulfur] cluster + 3 H2O = sulfite + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
redox reaction
-
-
-
-
reduction
additional information
-
sodium salts of thiosulfate and sulfate does not serve as the electron acceptor for reduced F420 oxidation by Fsr. Also, Fsr can not use NADH and NADPH for the reduction of sulfite.; the N-terminal half of Fsr represents a H2F420 dehydrogenase and the C-terminal half a dissimilatory-type siroheme sulfite reductase, and Fsr catalyzes the corresponding partial reactions
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
sulfate reduction II (assimilatory)
-
-
sulfate reduction
-
-
Sulfur metabolism
-
-
Metabolic pathways
-
-
Microbial metabolism in diverse environments
-
-
SYSTEMATIC NAME
IUBMB Comments
hydrogen-sulfide:ferredoxin oxidoreductase
An iron protein. The enzyme participates in sulfate assimilation. While it is usually found in cyanobacteria, plants and algae, it has also been reported in bacteria [4]. Different from EC 1.8.99.5, dissimilatory sulfite reductase, which is involved in prokaryotic sulfur-based energy metabolism. cf. EC 1.8.1.2, assimilatory sulfite reductase (NADPH).
CAS REGISTRY NUMBER
COMMENTARY hide
37256-50-1
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
cultivars Kojak, Encore, W202A, and Texas Grano
UniProt
Manually annotated by BRENDA team
DSM 4304T
-
-
Manually annotated by BRENDA team
strain OU-1
-
-
Manually annotated by BRENDA team
strain OU-1
-
-
Manually annotated by BRENDA team
var. Komatsuna
-
-
Manually annotated by BRENDA team
strain W5
-
-
Manually annotated by BRENDA team
strain W5
-
-
Manually annotated by BRENDA team
strain No. 9332
-
-
Manually annotated by BRENDA team
strain No. 9332
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
var. Sekitori No. 2
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
depletion of the enzyme results in chloroplast ablation
metabolism
physiological function
-
the enzyme plays a role in chloroplast-nucleoid metabolism, plastid gene expression, and thylakoid membrane development
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ammonium + oxidized ferredoxin + H2O
nitrite + reduced ferredoxin + H+
show the reaction diagram
-
-
-
-
?
hydrogen sulfide + oxidized ferredoxin + H2O
sulfite + reduced ferredoxin + H+
show the reaction diagram
-
-
-
-
?
S-sulfoglutathione + 6 reduced ferredoxin + 6 H+
glutathione persulfide + 6 oxidized ferredoxin + 3 H2O
show the reaction diagram
SO32- + FMNH2
S2- + FMN + H2O
show the reaction diagram
-
-
-
-
?
sulfite + 3 FMNH2
sulfide + 3 FMN + 3 H2O
show the reaction diagram
-
sulfate assimilation pathway leading to the biosynthesis of organic sulfur compounds
-
-
?
sulfite + methyl viologen
sulfide + ?
show the reaction diagram
-
-
-
?
sulfite + reduced coenzyme F420
sulfide + oxidized coenzyme F420
show the reaction diagram
-
-
-
-
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
show the reaction diagram
sulfite + reduced ferredoxin + 6 H+
sulfide + oxidized ferredoxin + 3 H2O
show the reaction diagram
-
sulfur assimilation for cysteine and methionine biosynthesis
-
-
?
sulfite + reduced ferredoxin + H+
hydrogen sulfide + oxidized ferredoxin + H2O
show the reaction diagram
sulfite + reduced methyl viologen + H+
hydrogen sulfide + oxidized methyl viologen + H2O
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
hydrogen sulfide + oxidized ferredoxin + H2O
sulfite + reduced ferredoxin + H+
show the reaction diagram
-
-
-
-
?
sulfite + 3 FMNH2
sulfide + 3 FMN + 3 H2O
show the reaction diagram
-
sulfate assimilation pathway leading to the biosynthesis of organic sulfur compounds
-
-
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
show the reaction diagram
sulfite + reduced ferredoxin + 6 H+
sulfide + oxidized ferredoxin + 3 H2O
show the reaction diagram
-
sulfur assimilation for cysteine and methionine biosynthesis
-
-
?
sulfite + reduced ferredoxin + H+
hydrogen sulfide + oxidized ferredoxin + H2O
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Fe-S center
Ferredoxin
-
iron-sulfur centre
-
-
siroheme
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4Fe-4S
tungstate
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cyanide
N-acetylsuccinimide
-
inhibition of the ferredoxin-linked activity without inhibiting the methyl viologen-linked activity
N-bromosuccinimide
-
treatment leads to a loss of enzymatic activity with reduced ferredoxin and reduced methyl viologen
Phenylglyoxal
-
inhibition of the ferredoxin-linked activity and the methyl viologen-linked activity
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
tungstic acid
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0017 - 0.076
Ferredoxin
-
0.221
nitrite
-
-
0.021
reduced coenzyme F420
-
at a fixed sulfite concentration of 0.29 mM and within a reduced coenzyme F420 concentration range of 0.004-0.06 mM
0.004 - 0.025
reduced ferredoxin
0.006
reduced methyl viologen
-
-
0.6
S-Sulfoglutathione
-
-
0.0087 - 0.22
sulfite
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.6 - 6
Ferredoxin
-
243
nitrite
Cyanidioschyzon merolae
-
-
2.1 - 3.65
reduced ferredoxin
2.4 - 9.1
sulfite
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0013
-
in 50 mM potassium phosphate buffer (pH 7), 0.044 mM reduced coenzyme F420, and 1.5 mM sodium sulfite, from cell extract
0.0182
-
in 50 mM potassium phosphate buffer (pH 7), 0.044 mM reduced coenzyme F420, and 1.5 mM sodium sulfite, after 14fold purification
5.09
-
sulfite as substrate
5.3
-
with reduced ferredoxin as the electron donor
8.9
-
69K enzyme
10.3
-
63K enzyme
44.6
-
sulfide
45.4
-
ferredoxin
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 8.8
-
Tris-phosphate buffer
7.5
-
activity assay
7.7
-
potassium phosphate buffer
7.8
-
potassium phosphate buffer
8 - 8.5
-
Tris-HCl buffer
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
-
enzyme assay, reduced methyl viologen as electron donor
30
-
enzyme assay
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
ferredoxin I and ferredoxin II
Manually annotated by BRENDA team
-
ferredoxin I and ferredoxin II
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
in seedling roots
Manually annotated by BRENDA team
-
grana in chloroplasts
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
18000
-
superdex-75 column, SDS-PAGE
20000
-
native enzime, superdex-75 column
27000
-
gel filtration
65000
-
three isoenzymes, gel filtration
66000
-
in presence of 200 mM NaCl, gel filtration
68000
-
in presence of 200 mM NaCl, gel filtration
112000 - 119000
-
63K enzyme, equilibrium sedimentation, gel filtration
120000
134000
-
69K enzyme, equilibrium sedimentation
137000
-
high ionic strength, gel filtration, at low ionic strength enzyme co-migrates with ferredoxin
350000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homooctamer
-
alpha8
monomer
tetramer
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4 * 136000, dimer of two dimers, in the presence of 200 mM NaCl, gel filtration, 4 * 71000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
no modification
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging-drop method, crystal structure of the dSir (alphabeta)2 core complex at 2.0 A resolution
-
hanging drop vapour diffusion method using 0.1 M Tris-HCl, pH range 8.2-8.7, 0.2 M MgCl2, and 30% polyethylene glycol 4000
hanging drop vapour diffusion method
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
-
no activity loss after heating for 5 h at this temperature, activity loss after incubation at 60C for 30 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
stable in 0.01 M phosphate buffer, pH 7.7
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, stable for 3 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; phenyl-sepharosa column, DNA cellulose column
-
ammonium sulfate precipitacion, filtration on a superdex-75 column
-
cell extract is treated with DEAE-cellulose in a batchwise manner, the unbound fraction is fractionated by ammonium sulfate precipitation, anion-exchange and hydrophobic column chromatography are applied
-
Ni2+-nitrilotriacetic acid affinity matrix and Q-Sepharose column chromatography
partially, crude leaves extract
-
phenyl-Sepharose chromatography, F420-Sepharose chromatography and QAE-Sephadex gel filtration
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
-
into the vector pTrc99A for expression in Escherichia coli cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
a significant increase in activity is observed in the leaves of the pungent cultivar Kojak in response to added sulfur but not in the less pungent cultivar Encore. In hydroponically-grown plants, levels of enzyme transcripts are significantly higher in the roots of sulfur-sufficient when compared with sulfur-deficient plants of the pungent cultivar W202A but not the less pungent cultivar Texas Grano 438. A higher level of enzyme activity is also observed in the sulfur-sufficient treatment in leaves of both cultivars before and after bulbing
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C161A
catalytically impaired mutant, tested in an assay using the nonphysiological electron donor methyl viologen and sulfite as substrate
C161S
catalytically impaired mutant, tested in an assay using the nonphysiological electron donor methyl viologen and sulfite as substrate
Y69A
catalytically impaired mutant, tested in an assay using the nonphysiological electron donor methyl viologen and sulfite as substrate
Y69F
catalytically impaired mutant, tested in an assay using the nonphysiological electron donor methyl viologen and sulfite as substrate
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
potential target for the development of antituberculosis agents
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