Information on EC 1.8.99.1 - sulfite reductase

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

EC NUMBER
COMMENTARY
1.8.99.1
-
RECOMMENDED NAME
GeneOntology No.
sulfite reductase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
hydrogen sulfide + acceptor + 3 H2O = sulfite + reduced acceptor
show the reaction diagram
an iron-protein. no products: trithionate, thiosulfate. A stochiometry of six molecules of reduced methyl viologen per molecule of sulfide formed is found. No products: trithionate, thiosulfate
-
-
-
hydrogen sulfide + acceptor + 3 H2O = sulfite + reduced acceptor
show the reaction diagram
mechanism, structure and kinetic of ligand-binding by siroheme
-
hydrogen sulfide + acceptor + 3 H2O = sulfite + reduced acceptor
show the reaction diagram
inducible by sulfate
-
hydrogen sulfide + acceptor + 3 H2O = sulfite + reduced acceptor
show the reaction diagram
cysteine represses the expression in vivo
-
hydrogen sulfide + acceptor + 3 H2O = sulfite + reduced acceptor
show the reaction diagram
mechanism
-
hydrogen sulfide + acceptor + 3 H2O = sulfite + reduced acceptor
show the reaction diagram
mechanism; mechanism, structure and kinetic of ligand-binding by siroheme
-
hydrogen sulfide + acceptor + 3 H2O = sulfite + reduced acceptor
show the reaction diagram
mechanism
-
hydrogen sulfide + acceptor + 3 H2O = sulfite + reduced acceptor
show the reaction diagram
mechanism; mechanism, structure and kinetic of ligand-binding by siroheme
Desulfovibrio vulgaris Hildenborough
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
oxidation
Q0A838 and Q0A837
-
oxidation
B8PT92 and B8PT93
-
oxidation
A1AXC9 and A1AXC8
-
oxidation
Candidatus Vesicomyosocius okutanii, Chlorobaculum tepidum, Chlorobium chlorochromatii
-
-
oxidation
B8PT99 and B8PTA0
-
oxidation
A1BCS1 and A1BCS2
-
oxidation
A4SC58 and A4SC59
-
oxidation
B8PTB5 and B8PTB6
-
oxidation
A1WYF3 and A1WYF4
-
oxidation
Magnetococcus sp.
-
-
oxidation
A4TYV1 and A4TYV0
-
oxidation
Q2W1V4 and Q2W1V3
-
oxidation
Q3SG18 and Q3SG19
-
oxidation
B8PTB3 and B8PTB4
-
oxidation
B8PTB0 and B8PTB1
-
oxidation
B8PTA5 and B8PTA6
-
oxidation
B8PT95 and B8PT96
-
oxidation
B8PTA1 and B8PTA2
-
oxidation
B8PT94
-
oxidation
B8PTA3 and B8PTA4
-
redox reaction
-
-
-
-
reduction
-
-
-
-
reduction
Q0A838 and Q0A837
-
reduction
B8PT92 and B8PT93
-
reduction
A1AXC9 and A1AXC8
-
reduction
Candidatus Vesicomyosocius okutanii, Chlorobaculum tepidum, Chlorobium chlorochromatii
-
-
reduction
B8PT99 and B8PTA0
-
reduction
A1BCS1 and A1BCS2
-
reduction
A4SC58 and A4SC59
-
reduction
B8PTB5 and B8PTB6
-
reduction
A1WYF3 and A1WYF4
-
reduction
Magnetococcus sp.
-
-
reduction
A4TYV1 and A4TYV0
-
reduction
Q2W1V4 and Q2W1V3
-
reduction
Q3SG18 and Q3SG19
-
reduction
B8PTB3 and B8PTB4
-
reduction
B8PTB0 and B8PTB1
-
reduction
B8PTA5 and B8PTA6
-
reduction
B8PT95 and B8PT96
-
reduction
B8PTA1 and B8PTA2
-
reduction
B8PT94
-
reduction
B8PTA3 and B8PTA4
-
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
KEGG Link
MetaCyc Link
Metabolic pathways
-
Microbial metabolism in diverse environments
-
sulfate reduction IV (dissimilatory)
-
Sulfur metabolism
-
sulfur oxidation IV (intracellular sulfur)
-
superpathway of tetrathionate reduction (Salmonella typhimurium)
-
superpathway of thiosulfate metabolism (Desulfovibrio sulfodismutans)
-
SYSTEMATIC NAME
IUBMB Comments
hydrogen-sulfide:acceptor oxidoreductase
An iron-protein. A stoichiometry of six molecules of reduced methyl viologen per molecule of sulfide formed was found.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
ASiR
Desulfovibrio vulgaris Hildenborough
-
-
-
assimilatory sulfite reductase
-
-
-
-
assimilatory sulfite reductase
-
-
assimilatory-type sulfite reductase
-
-
-
-
coenzyme F420-dependent sulfite reductase
-
-
desulfoviridin
-
formerly
desulfoviridin
Desulfovibrio vulgaris Miyazaki F
-
formerly
-
dissimilatory sulfite reductase
Q59109
-
dissimilatory sulfite reductase
O93650 and O93651
-
dissimilatory sulfite reductase
O93650 and O93651
-
-
dissimilatory sulfite reductase
-
-
dissimilatory sulfite reductase
Chlorobaculum tepidum CH-1
-
-
-
dissimilatory sulfite reductase
-
-
dissimilatory sulfite reductase
-
-
dissimilatory sulfite reductase
-
-
dissimilatory sulfite reductase
Desulfovibrio vulgaris Miyazaki F
-
-
-
dissimilatory sulfite reductase
E5DG53, E5DG55, E5DG56, E5DG57, E5DG58, E5DG59, E5DG60, E5DG61, E5DG62, E5DG63, E5DG64, E5DG65, E5DG66, E5DG67, E5DG68, E5DG69, E5DG71, E5DG72
-
dissimilatory sulfite reductase DsrAB
-
-
DSR
Chlorobaculum tepidum CH-1
-
-
-
DSR
Desulfovibrio vulgaris Miyazaki F
-
-
-
DSR
E5DG53, E5DG55, E5DG56, E5DG57, E5DG58, E5DG59, E5DG60, E5DG61, E5DG62, E5DG63, E5DG64, E5DG65, E5DG66, E5DG67, E5DG68, E5DG69, E5DG71, E5DG72
-
DsrAB
O93650 and O93651
-
DsrAB
O93650 and O93651
-
-
DsrABC
Desulfovibrio vulgaris Miyazaki F
-
-
-
F420-dependent sulfite reductase
-
-
rDSR
Q0A838 and Q0A837
-
rDSR
B8PT92 and B8PT93
-
rDSR
A1AXC9 and A1AXC8
-
rDSR
Candidatus Vesicomyosocius okutanii, Chlorobaculum tepidum, Chlorobium chlorochromatii
-
-
rDSR
B8PT99 and B8PTA0
-
rDSR
A1BCS1 and A1BCS2
-
rDSR
A4SC58 and A4SC59
-
rDSR
B8PTB5 and B8PTB6
-
rDSR
A1WYF3 and A1WYF4
-
rDSR
Magnetococcus sp.
-
-
rDSR
A4TYV1 and A4TYV0
-
rDSR
Q2W1V4 and Q2W1V3
-
rDSR
Q3SG18 and Q3SG19
-
rDSR
B8PTB3 and B8PTB4
-
rDSR
B8PTB0 and B8PTB1
-
rDSR
B8PTA5 and B8PTA6
-
rDSR
B8PT95 and B8PT96
-
rDSR
B8PTA1 and B8PTA2
-
rDSR
B8PT94
-
rDSR
B8PTA3 and B8PTA4
-
reductase, sulfite
-
-
-
-
reversely operating siroheme dissimilatory sulfite reductase
Q0A838 and Q0A837
-
reversely operating siroheme dissimilatory sulfite reductase
B8PT92 and B8PT93
-
reversely operating siroheme dissimilatory sulfite reductase
A1AXC9 and A1AXC8
-
reversely operating siroheme dissimilatory sulfite reductase
Candidatus Vesicomyosocius okutanii, Chlorobaculum tepidum, Chlorobium chlorochromatii
-
-
reversely operating siroheme dissimilatory sulfite reductase
B8PT99 and B8PTA0
-
reversely operating siroheme dissimilatory sulfite reductase
A1BCS1 and A1BCS2
-
reversely operating siroheme dissimilatory sulfite reductase
A4SC58 and A4SC59
-
reversely operating siroheme dissimilatory sulfite reductase
B8PTB5 and B8PTB6
-
reversely operating siroheme dissimilatory sulfite reductase
A1WYF3 and A1WYF4
-
reversely operating siroheme dissimilatory sulfite reductase
Magnetococcus sp.
-
-
reversely operating siroheme dissimilatory sulfite reductase
A4TYV1 and A4TYV0
-
reversely operating siroheme dissimilatory sulfite reductase
Q2W1V4 and Q2W1V3
-
reversely operating siroheme dissimilatory sulfite reductase
Q3SG18 and Q3SG19
-
reversely operating siroheme dissimilatory sulfite reductase
B8PTB3 and B8PTB4
-
reversely operating siroheme dissimilatory sulfite reductase
B8PTB0 and B8PTB1
-
reversely operating siroheme dissimilatory sulfite reductase
B8PTA5 and B8PTA6
-
reversely operating siroheme dissimilatory sulfite reductase
B8PT95 and B8PT96
-
reversely operating siroheme dissimilatory sulfite reductase
B8PTA1 and B8PTA2
-
reversely operating siroheme dissimilatory sulfite reductase
B8PT94
-
reversely operating siroheme dissimilatory sulfite reductase
B8PTA3 and B8PTA4
-
SIRHP
-
hemoprotein subunit of sulfite reductase
sulfite reductase
Q0A838 and Q0A837
-
sulfite reductase
B8PT92 and B8PT93
-
sulfite reductase
A1AXC9 and A1AXC8
-
sulfite reductase
Candidatus Vesicomyosocius okutanii, Chlorobaculum tepidum, Chlorobium chlorochromatii
-
-
sulfite reductase
B8PT99 and B8PTA0
-
sulfite reductase
A1BCS1 and A1BCS2
-
sulfite reductase
A4SC58 and A4SC59
-
sulfite reductase
-
-
sulfite reductase
B8PTB5 and B8PTB6
-
sulfite reductase
A1WYF3 and A1WYF4
-
sulfite reductase
Magnetococcus sp.
-
-
sulfite reductase
A4TYV1 and A4TYV0
-
sulfite reductase
Q2W1V4 and Q2W1V3
-
sulfite reductase
-
-
sulfite reductase
Q3SG18 and Q3SG19
-
sulfite reductase
B8PTB3 and B8PTB4
-
sulfite reductase
B8PTB0 and B8PTB1
-
sulfite reductase
B8PTA5 and B8PTA6
-
sulfite reductase
B8PT95 and B8PT96
-
sulfite reductase
B8PTA1 and B8PTA2
-
sulfite reductase
B8PT94
-
sulfite reductase
B8PTA3 and B8PTA4
-
sulphite reductase
-
-
sulphite reductase
-
-
additional information
-
a third type of sulfite reductase of low molecular range in sulfate-reducing bacteria, termed assimilatory because of reduction of sulfite to sulfide with high fidelity
CAS REGISTRY NUMBER
COMMENTARY
37256-51-2
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
alpha subunit DsrA and beta subunit DsrB
Q0A838 and Q0A837
UniProt
Manually annotated by BRENDA team
Allium odoratum
-
-
-
Manually annotated by BRENDA team
alpha subunit DsrA and beta subunit DsrB, fragments
B8PT92 and B8PT93
UniProt
Manually annotated by BRENDA team
ecotype Col-0
-
-
Manually annotated by BRENDA team
O93650: alpha-subunit, O93651: beta-subunit
O93650 and O93651
UniProt
Manually annotated by BRENDA team
O93650: alpha-subunit, O93651: beta-subunit
O93650 and O93651
UniProt
Manually annotated by BRENDA team
alpha subunit and beta subunit
A1AXC9 and A1AXC8
UniProt
Manually annotated by BRENDA team
Candidatus Vesicomyosocius okutanii
-
-
-
Manually annotated by BRENDA team
Chlorobaculum tepidum CH-1
-
-
-
Manually annotated by BRENDA team
alpha subunit DsrA and beta subunit DsrB, fragments
B8PT99 and B8PTA0
UniProt
Manually annotated by BRENDA team
alpha subunit and beta subunit
A1BCS1 and A1BCS2
UniProt
Manually annotated by BRENDA team
alpha subunit and beta subunit
A4SC58 and A4SC59
UniProt
Manually annotated by BRENDA team
strain PM. and T
-
-
Manually annotated by BRENDA team
Chlorobium sp. PM.
strain PM. and T
-
-
Manually annotated by BRENDA team
Chromatium sp.
strain D
-
-
Manually annotated by BRENDA team
Chromatium sp. D
strain D
-
-
Manually annotated by BRENDA team
Desulfovibrio vulgaris Hildenborough, ATCC 29579
-
-
Manually annotated by BRENDA team
Desulfovibrio vulgaris Hildenborough, DSM 644
-
-
Manually annotated by BRENDA team
Desulfovibrio vulgaris Hildenborough, DSM 644; DSM 644, Hildenborough
-
-
Manually annotated by BRENDA team
Desulfovibrio vulgaris Hildenborough
Hildenborough
-
-
Manually annotated by BRENDA team
Desulfovibrio vulgaris Miyazaki F
-
-
-
Manually annotated by BRENDA team
complex of flavoprotein component and haemoprotein component
-
-
Manually annotated by BRENDA team
alpha subunit DsrA and beta subunit DsrB, fragments
B8PTB5 and B8PTB6
UniProt
Manually annotated by BRENDA team
alpha subunit and beta subunit
A1WYF3 and A1WYF4
UniProt
Manually annotated by BRENDA team
Magnetococcus sp.
-
-
-
Manually annotated by BRENDA team
alpha subunit DsrA and beta subunit DsrB
A4TYV1 and A4TYV0
UniProt
Manually annotated by BRENDA team
alpha subunit and beta subunit
Q2W1V4 and Q2W1V3
UniProt
Manually annotated by BRENDA team
red algae
-
-
Manually annotated by BRENDA team
strain Hefix
-
-
Manually annotated by BRENDA team
Saccharomyces bayanus Hefix
strain Hefix
-
-
Manually annotated by BRENDA team
commercial wine yeast
-
-
Manually annotated by BRENDA team
strain Johannisberg; strain Johannisberg Riesling; strain Johannisberg sulfite; strain Syrena; strain Tokay; strain Tokay sulfite
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae Johannisberg
strain Johannisberg; strain Johannisberg Riesling
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae Johannisberg sulfite
strain Johannisberg sulfite
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae Syrena
strain Syrena
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae Tokay
strain Tokay
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae Tokay sulfite
strain Tokay sulfite
-
-
Manually annotated by BRENDA team
strain PCC7942
-
-
Manually annotated by BRENDA team
Synechococcus sp. PCC7942
strain PCC7942
-
-
Manually annotated by BRENDA team
alpha subunit and beta subunit
Q3SG18 and Q3SG19
UniProt
Manually annotated by BRENDA team
alpha subunit DsrA and beta subunit DsrB
B8PTB3 and B8PTB4
UniProt
Manually annotated by BRENDA team
alpha subunit DsrA and beta subunit DsrB, fragments
B8PTB0 and B8PTB1
UniProt
Manually annotated by BRENDA team
alpha subunit DsrA and beta subunit DsrB, fragments
B8PTA5 and B8PTA6
UniProt
Manually annotated by BRENDA team
alpha subunit DsrA and beta subunit DsrB, fragments
B8PT95 and B8PT96
UniProt
Manually annotated by BRENDA team
alpha subunit DsrA and beta subunit DsrB, fragments
B8PTA1 and B8PTA2
UniProt
Manually annotated by BRENDA team
beta subunit DsrB, fragment
UniProt
Manually annotated by BRENDA team
alpha subunit DsrA and beta subunit DsrB, fragments
B8PTA3 and B8PTA4
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
-
dissimilatory sulfite reductase mutants incapable of complete substrate oxidation oxidize sulfide and thiosulfate about twice as fast as the wild type, while having only slightly lower growth rates (70-80% of wild type)
malfunction
-
enzyme downregulation causes severe adaptive reactions of primary and secondary metabolism. Seedlings with 14% transcript levels compared with the wild type are early seedling lethal, while seedlings having 44% transcript levels are viable but strongly retarded in growth. Enzyme downregulation result in a higher sensitivity toward cadmium (2.6fold)
malfunction
Chlorobaculum tepidum CH-1
-
dissimilatory sulfite reductase mutants incapable of complete substrate oxidation oxidize sulfide and thiosulfate about twice as fast as the wild type, while having only slightly lower growth rates (70-80% of wild type)
-
metabolism
-
sulfur globule oxidation is strictly dependent on the dissimilatory sulfite reductase (DSR). The DSR system is dispensable in environments with sufficiently high sulfide concentrations
metabolism
Chlorobaculum tepidum CH-1
-
sulfur globule oxidation is strictly dependent on the dissimilatory sulfite reductase (DSR). The DSR system is dispensable in environments with sufficiently high sulfide concentrations
-
physiological function
-, O93650 and O93651
the enzyme catalyzes the terminal step in the reduction of sulfate to sulfide
physiological function
-
optimal enzyme activity is essential for normal development growth
physiological function
-
the enzyme catalyzes the terminal step in the reduction of sulfate to sulfide
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
HSO3- + 3 H2
HS- + 3 H2O
show the reaction diagram
-
pathways of elemental sulfur and thiosulfate disproportionation
-
-
?
HSO3- + H2
HS- + H2O
show the reaction diagram
-
-
-
-
?
hydrogen sulfide + acceptor + H2O
sulfite + reduced acceptor
show the reaction diagram
-
-
-
-
?
hydroxylamine + reduced methyl viologen
?
show the reaction diagram
-
-
-
-
?
hydroxylamine + reduced methyl viologen
?
show the reaction diagram
-
-
-
-
?
hydroxylamine + reduced methyl viologen
?
show the reaction diagram
-
-
-
-
?
hydroxylamine + reduced methyl viologen
?
show the reaction diagram
-
-
-
-
?
hydroxylamine + reduced methyl viologen
?
show the reaction diagram
Desulfovibrio vulgaris Hildenborough
-
-
-
-
?
hydroxylamine + reduced methyl viologen + H+
ammonia + oxidized methyl viologen + ?
show the reaction diagram
-
-
-
-
?
nitrite + reduced methyl viologen
NH4+ + oxidized methyl viologen
show the reaction diagram
-
-
-
-
?
nitrite + reduced methyl viologen
NH4+ + oxidized methyl viologen
show the reaction diagram
-
-
-
-
?
nitrite + reduced methyl viologen
NH4+ + oxidized methyl viologen
show the reaction diagram
-
higher reactivity than with sulfite
-
?
nitrite + reduced methyl viologen
NH4+ + oxidized methyl viologen
show the reaction diagram
-
higher reactivity than with sulfite
-
-
?
nitrite + reduced methyl viologen
NH4+ + oxidized methyl viologen
show the reaction diagram
Desulfovibrio vulgaris Hildenborough
-
-
-
-
?
nitrite + reduced methyl viologen + H+
ammonia + oxidized methyl viologen + ?
show the reaction diagram
Q59109
-
-
-
?
SO2 + NADPH
SH2 + NADP+
show the reaction diagram
Saccharomyces cerevisiae, Saccharomyces bayanus, Saccharomyces cerevisiae Syrena, Saccharomyces cerevisiae Tokay sulfite, Saccharomyces cerevisiae Johannisberg, Saccharomyces cerevisiae Johannisberg sulfite, Saccharomyces bayanus Hefix, Saccharomyces cerevisiae Tokay
-
-
-
-
?
sulfite + acceptor
hydrogen sulfide + acceptor + H2O
show the reaction diagram
Chlorobaculum tepidum, Chlorobaculum tepidum CH-1
-
-
-
-
?
sulfite + NADPH + 6 H+
sulfide + NADP+ + 3 H2O
show the reaction diagram
Saccharomyces cerevisiae, Saccharomyces bayanus, Saccharomyces cerevisiae Syrena, Saccharomyces cerevisiae Tokay sulfite, Saccharomyces cerevisiae Johannisberg, Saccharomyces cerevisiae Johannisberg sulfite, Saccharomyces bayanus Hefix, Saccharomyces cerevisiae Tokay
-
sulfide synthesis for incorporation into sulfur-containing amino acids and enzyme cofactors
-
-
?
sulfite + reduced acceptor
sulfide + oxidized acceptor
show the reaction diagram
-
-
-
?
sulfite + reduced acceptor
sulfide + oxidized acceptor
show the reaction diagram
-
-
-
?
sulfite + reduced acceptor
sulfide + oxidized acceptor
show the reaction diagram
-
-
-
?
sulfite + reduced acceptor
sulfide + oxidized acceptor
show the reaction diagram
-
-
-
?
sulfite + reduced acceptor
sulfide + oxidized acceptor
show the reaction diagram
-
-
-
?
sulfite + reduced acceptor
sulfide + oxidized acceptor
show the reaction diagram
-
-
-
?
sulfite + reduced acceptor
sulfide + oxidized acceptor
show the reaction diagram
-
-
-
?
sulfite + reduced acceptor
sulfide + oxidized acceptor
show the reaction diagram
-
-
-
?
sulfite + reduced acceptor
sulfide + oxidized acceptor
show the reaction diagram
-
-
-
?
sulfite + reduced acceptor
sulfide + oxidized acceptor
show the reaction diagram
-
-
-
r
sulfite + reduced acceptor
sulfide + oxidized acceptor
show the reaction diagram
E5DG53, E5DG55, E5DG56, E5DG57, E5DG58, E5DG59, E5DG60, E5DG61, E5DG62, E5DG63, E5DG64, E5DG65, E5DG66, E5DG67, E5DG68, E5DG69, E5DG71, E5DG72
-
-
-
?
sulfite + reduced acceptor
sulfide + oxidized acceptor
show the reaction diagram
-
specific, e.g. methyl viologen, sole artificial electron donor for Desulfovibrio vulgaris enzyme
-
?
sulfite + reduced acceptor
sulfide + oxidized acceptor
show the reaction diagram
-
ferredoxin as electron acceptor
-
?
sulfite + reduced acceptor
sulfide + oxidized acceptor
show the reaction diagram
-
reduced methyl viologen as electron donor
-
?
sulfite + reduced acceptor
sulfide + oxidized acceptor
show the reaction diagram
-
reduced methyl viologen as electron donor
-
?
sulfite + reduced acceptor
sulfide + oxidized acceptor
show the reaction diagram
-
reduced methyl viologen as electron donor
-
?
sulfite + reduced acceptor
sulfide + oxidized acceptor
show the reaction diagram
-
reduced methyl viologen as electron donor
-
?
sulfite + reduced acceptor
sulfide + oxidized acceptor
show the reaction diagram
-
reduced methyl viologen as electron donor
-
?
sulfite + reduced acceptor
sulfide + oxidized acceptor
show the reaction diagram
-
reduced methyl viologen as electron donor
-
?
sulfite + reduced acceptor
sulfide + oxidized acceptor
show the reaction diagram
-
reduced methyl viologen as electron donor
-
?
sulfite + reduced acceptor
sulfide + oxidized acceptor
show the reaction diagram
-
reduced methyl viologen as electron donor
-
?
sulfite + reduced acceptor
sulfide + oxidized acceptor
show the reaction diagram
-
reduced methyl viologen as electron donor
-
?
sulfite + reduced acceptor
sulfide + oxidized acceptor
show the reaction diagram
-
reduced methyl viologen as electron donor
-
?
sulfite + reduced acceptor
sulfide + oxidized acceptor
show the reaction diagram
-
reduced methyl viologen as electron donor
-
?
sulfite + reduced acceptor
sulfide + oxidized acceptor
show the reaction diagram
-
reduced methyl viologen as electron donor
-
?
sulfite + reduced acceptor
sulfide + oxidized acceptor
show the reaction diagram
-
reduced methyl viologen as electron donor
-
?
sulfite + reduced acceptor
sulfide + oxidized acceptor
show the reaction diagram
Pyropia yezoensis, Allium odoratum
-
reduced methyl viologen as electron donor
-
?
sulfite + reduced acceptor
sulfide + oxidized acceptor
show the reaction diagram
-
electron donor benzyl viologen
-
?
sulfite + reduced acceptor
sulfide + oxidized acceptor
show the reaction diagram
-
electron donor benzyl viologen
-
?
sulfite + reduced acceptor
sulfide + oxidized acceptor
show the reaction diagram
-
electron donor benzyl viologen, electron donors: phenazine methosulfate, janus green, methylene blue, nile blue, and toluidine blue
-
?
sulfite + reduced acceptor
sulfide + oxidized acceptor
show the reaction diagram
-
riboflavin, 3-acetylpyridine adenine dinucleotide phosphate, or ferricyanide as electron acceptors
-
?
sulfite + reduced acceptor
sulfide + oxidized acceptor
show the reaction diagram
-
Dsr catalyzes a six-electron reduction converting sulfite to sulfide
-
-
?
sulfite + reduced acceptor
sulfide + oxidized acceptor
show the reaction diagram
Chlorobium sp. PM., Chromatium sp. D
-
reduced methyl viologen as electron donor
-
?
sulfite + reduced acceptor
sulfide + oxidized acceptor
show the reaction diagram
Desulfovibrio vulgaris Miyazaki F
-
Dsr catalyzes a six-electron reduction converting sulfite to sulfide
-
-
?
sulfite + reduced acceptor
sulfide + oxidized acceptor
show the reaction diagram
Desulfovibrio vulgaris Hildenborough
-
-
-
r
sulfite + reduced acceptor
sulfide + oxidized acceptor
show the reaction diagram
Desulfovibrio vulgaris Hildenborough
-
-
-
?
sulfite + reduced acceptor
sulfide + oxidized acceptor
show the reaction diagram
Desulfovibrio vulgaris Hildenborough
-
reduced methyl viologen as electron donor
-
?
sulfite + reduced acceptor
sulfide + oxidizied acceptor
show the reaction diagram
-
-
-
-
?
sulfite + reduced acceptor
sulfide + oxidizied acceptor
show the reaction diagram
-
-
-
-
?
sulfite + reduced acceptor
sulfide + oxidizied acceptor
show the reaction diagram
-
-
-
-
?
sulfite + reduced acceptor
sulfide + oxidizied acceptor
show the reaction diagram
-
-
-
-
?
sulfite + reduced acceptor
sulfide + oxidizied acceptor
show the reaction diagram
-
-
-
-
?
sulfite + reduced acceptor
sulfide + oxidizied acceptor
show the reaction diagram
-
physiological acceptor: e.g. cytochrome P450 or sulphite reductase haemoprotein
-
-
?
sulfite + reduced acceptor
sulfide + oxidizied acceptor
show the reaction diagram
-
intermediate step of assimiliatory reduction of sulfate to the SH level
-
-
?
sulfite + reduced acceptor
sulfide + oxidizied acceptor
show the reaction diagram
-
intermediate step of assimiliatory reduction of sulfate to the SH level
-
-
?
sulfite + reduced acceptor
sulfide + oxidizied acceptor
show the reaction diagram
-
intermediate step of assimiliatory reduction of sulfate to the SH level
-
-
?
sulfite + reduced acceptor
sulfide + oxidizied acceptor
show the reaction diagram
-
intermediate step of assimiliatory reduction of sulfate to the SH level
-
-
?
sulfite + reduced acceptor
sulfide + oxidizied acceptor
show the reaction diagram
-
intermediate step of assimiliatory reduction of sulfate to the SH level
-
-
?
sulfite + reduced acceptor
sulfide + oxidizied acceptor
show the reaction diagram
Pyropia yezoensis, Allium odoratum
-
intermediate step of assimiliatory reduction of sulfate to the SH level
-
-
?
sulfite + reduced acceptor
sulfide + oxidizied acceptor
show the reaction diagram
-
key enzyme in sulfate-assimilation and integration of sulfur into cysteine
-
-
?
sulfite + reduced acceptor
sulfide + oxidizied acceptor
show the reaction diagram
-
assimilatory sulfate reduction during biosynthesis of cell material
-
-
?
sulfite + reduced acceptor
sulfide + oxidizied acceptor
show the reaction diagram
-
assimilatory sulfate reduction during biosynthesis of cell material
-
-
?
sulfite + reduced acceptor
sulfide + oxidizied acceptor
show the reaction diagram
-
assimilatory sulfate reduction during biosynthesis of cell material
-
-
?
sulfite + reduced acceptor
sulfide + oxidizied acceptor
show the reaction diagram
-
involved in the assimilatory synthesis of sulfur-containing compounds
-
-
?
sulfite + reduced acceptor
sulfide + oxidizied acceptor
show the reaction diagram
Chlorobium sp. PM., Chromatium sp. D
-
assimilatory sulfate reduction during biosynthesis of cell material
-
-
?
sulfite + reduced acceptor
sulfide + oxidizied acceptor
show the reaction diagram
Desulfovibrio vulgaris Hildenborough
-
-
-
-
?
sulfite + reduced acceptor
sulfide + oxidizied acceptor
show the reaction diagram
Desulfovibrio vulgaris Hildenborough
-
assimilatory sulfate reduction during biosynthesis of cell material
-
-
?
sulfite + reduced acceptor
sulfide + oxidizied acceptor
show the reaction diagram
Desulfovibrio vulgaris Hildenborough
-
involved in the assimilatory synthesis of sulfur-containing compounds
-
-
?
sulfite + reduced coenzyme F420
sulfide + oxidized coenzyme F420
show the reaction diagram
-
-
-
-
?
sulfite + reduced F420
sulfide + oxidized F420
show the reaction diagram
-
-
-
-
?
sulfite + reduced methyl viologen + H+
hydrogen sulfide + oxidized methyl viologen + H2O
show the reaction diagram
Q59109
six-electron reduction of sulfite
-
-
?
sulfite + reduced methyl viologen + H+
hydrogen sulfide + methyl viologen + H2O
show the reaction diagram
-
-
-
-
?
sulfite + reduced methyl viologen+ H+
hydrogen sulfide + methyl viologen + H2O
show the reaction diagram
-
-
-
-
?
thiosulfate + reduced methyl viologen + H+
? + oxidized methyl viologen + H2O
show the reaction diagram
Q59109
thiosulfate exhibits a slightly higher activity than sulfite
-
-
?
trithionate + reduced methyl viologen + H+
? + oxidized methyl viologen + H2O
show the reaction diagram
Q59109
trithionate is less active than sulfite
-
-
?
hydroxylamine + reduced methyl viologen + H+
ammonia + oxidized methyl viologen + ?
show the reaction diagram
Q59109
-
-
-
?
additional information
?
-
-
no substrates: neutral red, phenosafranine, janus green, nile blue, methylene blue, toluidine blue, thionine, phenazine methosulfate, FMN, FAD, riboflavin, cytochrome c3, ferredoxin, NAD(P)H
-
-
-
additional information
?
-
-
the activity of the dissimilatory sulfite reductase regulates the kinetic isotope fractionation of sulfur and oxygen during bacterial sulfate reduction. Isotope fractionation during bacterial sulfate reduction strongly depends on the cell internal enzymatic regulation rather than on the physico-chemical features of the individual enzymes
-
-
-
additional information
?
-
-
catalyzes the final step in sulfate reduction
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
HSO3- + 3 H2
HS- + 3 H2O
show the reaction diagram
-
pathways of elemental sulfur and thiosulfate disproportionation
-
-
?
sulfite + acceptor
hydrogen sulfide + acceptor + H2O
show the reaction diagram
Chlorobaculum tepidum, Chlorobaculum tepidum CH-1
-
-
-
-
?
sulfite + NADPH + 6 H+
sulfide + NADP+ + 3 H2O
show the reaction diagram
Saccharomyces cerevisiae, Saccharomyces bayanus, Saccharomyces cerevisiae Syrena, Saccharomyces cerevisiae Tokay sulfite, Saccharomyces cerevisiae Johannisberg, Saccharomyces cerevisiae Johannisberg sulfite, Saccharomyces bayanus Hefix, Saccharomyces cerevisiae Tokay
-
sulfide synthesis for incorporation into sulfur-containing amino acids and enzyme cofactors
-
-
?
sulfite + reduced acceptor
sulfide + oxidizied acceptor
show the reaction diagram
-
-
-
-
?
sulfite + reduced acceptor
sulfide + oxidizied acceptor
show the reaction diagram
-
-
-
-
?
sulfite + reduced acceptor
sulfide + oxidizied acceptor
show the reaction diagram
-
-
-
-
?
sulfite + reduced acceptor
sulfide + oxidizied acceptor
show the reaction diagram
-
-
-
-
?
sulfite + reduced acceptor
sulfide + oxidizied acceptor
show the reaction diagram
-
-
-
-
?
sulfite + reduced acceptor
sulfide + oxidizied acceptor
show the reaction diagram
-
physiological acceptor: e.g. cytochrome P450 or sulphite reductase haemoprotein
-
-
?
sulfite + reduced acceptor
sulfide + oxidizied acceptor
show the reaction diagram
-
intermediate step of assimiliatory reduction of sulfate to the SH level
-
-
?
sulfite + reduced acceptor
sulfide + oxidizied acceptor
show the reaction diagram
-
intermediate step of assimiliatory reduction of sulfate to the SH level
-
-
?
sulfite + reduced acceptor
sulfide + oxidizied acceptor
show the reaction diagram
-
intermediate step of assimiliatory reduction of sulfate to the SH level
-
-
?
sulfite + reduced acceptor
sulfide + oxidizied acceptor
show the reaction diagram
-
intermediate step of assimiliatory reduction of sulfate to the SH level
-
-
?
sulfite + reduced acceptor
sulfide + oxidizied acceptor
show the reaction diagram
-
intermediate step of assimiliatory reduction of sulfate to the SH level
-
-
?
sulfite + reduced acceptor
sulfide + oxidizied acceptor
show the reaction diagram
Pyropia yezoensis, Allium odoratum
-
intermediate step of assimiliatory reduction of sulfate to the SH level
-
-
?
sulfite + reduced acceptor
sulfide + oxidizied acceptor
show the reaction diagram
-
key enzyme in sulfate-assimilation and integration of sulfur into cysteine
-
-
?
sulfite + reduced acceptor
sulfide + oxidizied acceptor
show the reaction diagram
-
assimilatory sulfate reduction during biosynthesis of cell material
-
-
?
sulfite + reduced acceptor
sulfide + oxidizied acceptor
show the reaction diagram
-
assimilatory sulfate reduction during biosynthesis of cell material
-
-
?
sulfite + reduced acceptor
sulfide + oxidizied acceptor
show the reaction diagram
-
assimilatory sulfate reduction during biosynthesis of cell material
-
-
?
sulfite + reduced acceptor
sulfide + oxidizied acceptor
show the reaction diagram
-
involved in the assimilatory synthesis of sulfur-containing compounds
-
-
?
sulfite + reduced acceptor
sulfide + oxidizied acceptor
show the reaction diagram
Chlorobium sp. PM., Chromatium sp. D
-
assimilatory sulfate reduction during biosynthesis of cell material
-
-
?
sulfite + reduced acceptor
sulfide + oxidizied acceptor
show the reaction diagram
Desulfovibrio vulgaris Hildenborough
-
-
-
-
?
sulfite + reduced acceptor
sulfide + oxidizied acceptor
show the reaction diagram
Desulfovibrio vulgaris Hildenborough
-
assimilatory sulfate reduction during biosynthesis of cell material
-
-
?
sulfite + reduced acceptor
sulfide + oxidizied acceptor
show the reaction diagram
Desulfovibrio vulgaris Hildenborough
-
involved in the assimilatory synthesis of sulfur-containing compounds
-
-
?
sulfite + reduced methyl viologen + H+
hydrogen sulfide + methyl viologen + H2O
show the reaction diagram
-
-
-
-
?
hydrogen sulfide + acceptor + H2O
sulfite + reduced acceptor
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
the activity of the dissimilatory sulfite reductase regulates the kinetic isotope fractionation of sulfur and oxygen during bacterial sulfate reduction. Isotope fractionation during bacterial sulfate reduction strongly depends on the cell internal enzymatic regulation rather than on the physico-chemical features of the individual enzymes
-
-
-
additional information
?
-
-
catalyzes the final step in sulfate reduction
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
3-acetylpyridine adenine dinucleotide
-
-
4Fe-4S-center
Q59109
the enzyme hosts a unique siroheme-[4Fe-4S] cofactor
FAD
-
electron transfer cascade: NADPH reduces FAD, which reduces FMN, FMNH2 reduces the physiological acceptor, e.g. cytochrome P450 or the sulphite reductase haemoprotein, in a catalytic cycle
Ferredoxin
-
-
-
Ferredoxin
-
-
-
Ferredoxin
-
-
-
FMN
-
electron transfer cascade: NADPH reduces FAD, which reduces FMN, FMNH2 reduces the physiological acceptor, e.g. cytochrome P450 or the sulphite reductase haemoprotein, in a catalytic cycle
heme
-
the enzyme contains two sirohemes
heme
Q59109
the enzyme hosts a unique siroheme-[4Fe-4S] cofactor
iron tetrahydroporphyrin
-
i.e. siroheme
iron tetrahydroporphyrin
-
i.e. siroheme
iron tetrahydroporphyrin
-
i.e. siroheme
NADPH
-
electron transfer cascade: NADPH reduces FAD, which reduces FMN, FMNH2 reduces the physiological acceptor, e.g. cytochrome P450 or the sulphite reductase haemoprotein, in a catalytic cycle
[4Fe-4S]-center
-
-
-
iron-sulfur centre
-
the enzyme contains eight Fe-S clusters
additional information
-
not NAD(P)H as electron donor; not reduced ferredoxin as electron donor
-
additional information
-
not NAD(P)H as electron donor
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Cu
-
contains Cu
Fe
-
[4Fe-4S]-siroheme prosthetic center; comparison of reduction potentials of siroheme and siroheme-[4Fe-4S] cluster, pH-dependency
Fe
-
contains Fe
Fe
-
contains Fe
Fe
-
1 4Fe-4S center per mol of enzyme
Fe
-
0.7 4Fe4S cluster per hemoprotein component
Fe
-
4.9 iron-centers per mol of enzyme and 5.1 sulfide per mole of enzyme
Fe
-
contains Fe; iron tetrahydroporphyrin prosthetic group, termed siroheme, in addition to nonheme iron in 4Fe-4S clusters, 4.7 iron atoms per mol of enzyme and 4.6 mol of acid-labile sulfur atoms per mol of enzyme
Fe
-
overview about alpha-beta subunit structure, topology and iron bound, a siroheme is coupled covalently to an 4Fe-4S-cluster
Fe
-
4Fe-4S-cluster
Mg2+
-
essentiell for activity
additional information
-
no Co, Mn, Mo, Zn
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
8-hydroxyquinoline
-
slight inhibition
diethyldithiocarbamate
-
slight inhibition
EDTA
-
slight inhibition
iodonium diphenyl chloride
-
covalent phenylation of FAD cofactor
N-ethylmaleimide
-
slight inhibition
Na2S
-
concentration above 1 mM
NH4+
-
an excess and an absence of SO2 corresponded to the relatively low activity
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
no inhibition
Tris-HCl
-
partially inhibited the enzyme
additional information
-
not inhibitory: thiourea, NH2NH2, atabrin, CuSO4, NaN3
-
additional information
-
inhibition via reduced cofactors
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
additional information
-
activation of low-molecular weight assmilatory sulfite reductases may also be related to exchange of a heme axial ligand; activation via reduced cofactors
-
additional information
-
activation via reduced cofactors
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.19
-
3-acetylpyridine adenine dinucleotide
-
with NADPH in electron transfer cycle
10.5
-
hydroxylamine
-
-
14
-
hydroxylamine
-
-
14
-
hydroxylamine
-
-
14
-
hydroxylamine
-
-
18
-
hydroxylamine
-
recombinant enzyme
20
-
hydroxylamine
-
-
0.088
-
NADPH
-
with riboflavin in electron transfer cycle
4.2
-
nitrite
-
recombinant enzyme
0.021
-
reduced F420
-
at a fixed sulfite concentration of 0.29 mM and within a reduced F420 concentration range of 0.004-0.06 mM
0.066
-
riboflavin
-
with NADPH in electron transfer cycle
0.0122
-
sulfite
-
within a sulfite concentration range of 0.0014-0.3 mM and with a fixed reduced F420 concentration of 0.04 mM
0.0167
0.0675
sulfite
-
30 C, pH 7.3
0.025
-
sulfite
-
-
0.055
-
sulfite
-
recombinant enzyme
0.65
-
sulfite
-
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
81
-
hydroxylamine
-
-
100
-
hydroxylamine
-
-
580
-
hydroxylamine
-
electrons per heme per sec
750
-
hydroxylamine
-
electrons per heme per sec; hemoprotein component
2300
-
hydroxylamine
-
-
2400
-
hydroxylamine
-
recombinant enzyme
4600
-
hydroxylamine
-
electrons per heme per sec
0.45
-
nitrite
-
-
4.4
-
nitrite
-
-
23
-
nitrite
-
recombinant enzyme
95
-
nitrite
-
-
98.3
-
nitrite
-
electrons per heme per sec; hemoprotein component
120
-
nitrite
-
electrons per heme per sec
0.19
-
sulfite
-
recombinant enzyme
0.2
-
sulfite
-
-
0.51
-
sulfite
-
-
1.3
-
sulfite
-
electrons per heme per sec
11
-
sulfite
-
electrons per heme per sec
43.3
-
sulfite
-
electrons per heme per sec; hemoprotein component
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0185
-
iodonium diphenyl chloride
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.0013
-
-
in 50 mM potassium phosphate buffer (pH 7), 0.044 mM reduced F420, and 1.5 mM sodium sulfite, from cell extract
0.0026
-
-
strain T
0.0042
-
Chromatium sp.
-
-
0.007
-
-
strain P.M.
0.0125
-
Q59109
at 83C, pH 7.0, using nitrite as substrate
0.0182
-
-
in 50 mM potassium phosphate buffer (pH 7), 0.044 mM reduced F420, and 1.5 mM sodium sulfite, after 14fold purification
0.0562
-
Q59109
at 83C, pH 7.0, using sulfite as substrate
6.5
-
-
native holoenzyme
11.5
-
-
purified flavoprotein component
17.5
-
-
sulfate-induced wild-type
additional information
-
-
activity on different assimilable nitrogen sources
additional information
-
-
0.002883 U/mg protein
additional information
-
-
0.001697 U/mg protein; 0.002250 U/mg protein; 0.002283 U/mg protein; 0.0026 U/mg protein; 0.003666 U/mg protein; 0.003750 U/mg protein
additional information
-
-
50 mU/mg of purified enzyme, 70 mU/mg of crude extract
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
-
Q59109
for the reduction of sulfite, thiosulfate, and trithionate
7.2
7.8
-
Tris-HCl buffer
8
-
-
above, phosphate buffer
additional information
-
-
comparison of pH-dependency of reduction potentials of siroheme and siroheme-[4Fe-4S] cluster
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
8
-
10% of relative activity at pH 6.45 and 50% of relative activity at pH 8.02
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-
assay at
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
8
-
-
30-50% of maximum activity
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
Saccharomyces bayanus Hefix, Saccharomyces cerevisiae Johannisberg, Saccharomyces cerevisiae Johannisberg sulfite, Saccharomyces cerevisiae Syrena, Saccharomyces cerevisiae Tokay, Saccharomyces cerevisiae Tokay sulfite
-
-
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Desulfovibrio vulgaris Miyazaki F
-
-
-
Manually annotated by BRENDA team
Chlorobium sp. PM., Chromatium sp. D, Desulfovibrio vulgaris Hildenborough
-
-
-
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
23500
-
-
gel filtration
26800
-
-
sedimentation equilibrium
27200
-
-
amino acid composition
40000
-
-
DsrB, monomer, determined by native-PAGE
50000
-
-
DsrA, monomer, determined by native-PAGE
84000
87000
-
gel filtration
180000
-
-
tetramer, alpha2beta2 arrangement, two subunits DsrA and DsrB, 2* 50000 + 2 * 40000
200000
-
-
tetramer, alpha2beta2 arrangement, two subunits DsrA and DsrB
350000
-
-
gel filtration
780000
-
-
sulfite reductase both flavoprotein and haemoprotein component, gel filtration
additional information
-
-
overview
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 14000, calculated from amino acid sequence
?
Chlorobaculum tepidum CH-1
-
x * 14000, calculated from amino acid sequence
-
heterohexamer
-
2 * 53000 + 2 * 42000 + 2 * 8000
heterohexamer
Desulfovibrio vulgaris Miyazaki F
-
2 * 53000 + 2 * 42000 + 2 * 8000
-
heterotetramer
-
2 * 51000 + 2 * 45000
heterotetramer
Q0A838 and Q0A837
alpha2beta2 quaternary structure
heterotetramer
B8PT92 and B8PT93
alpha2beta2 quaternary structure
heterotetramer
A1AXC9 and A1AXC8
alpha2beta2 quaternary structure
heterotetramer
Candidatus Vesicomyosocius okutanii, Chlorobaculum tepidum, Chlorobium chlorochromatii
-
alpha2beta2 quaternary structure
heterotetramer
B8PT99 and B8PTA0
alpha2beta2 quaternary structure
heterotetramer
A1BCS1 and A1BCS2
alpha2beta2 quaternary structure
heterotetramer
A4SC58 and A4SC59
alpha2beta2 quaternary structure
heterotetramer
B8PTB5 and B8PTB6
alpha2beta2 quaternary structure
heterotetramer
A1WYF3 and A1WYF4
alpha2beta2 quaternary structure
heterotetramer
Magnetococcus sp.
-
alpha2beta2 quaternary structure
heterotetramer
A4TYV1 and A4TYV0
alpha2beta2 quaternary structure
heterotetramer
Q2W1V4 and Q2W1V3
alpha2beta2 quaternary structure
heterotetramer
Q3SG18 and Q3SG19
alpha2beta2 quaternary structure
heterotetramer
B8PTB3 and B8PTB4
alpha2beta2 quaternary structure
heterotetramer
B8PTB0 and B8PTB1
alpha2beta2 quaternary structure
heterotetramer
B8PTA5 and B8PTA6
alpha2beta2 quaternary structure
heterotetramer
B8PT95 and B8PT96
alpha2beta2 quaternary structure
heterotetramer
B8PTA1 and B8PTA2
alpha2beta2 quaternary structure
heterotetramer
B8PT94
alpha2beta2 quaternary structure
heterotetramer
B8PTA3 and B8PTA4
alpha2beta2 quaternary structure
heterotetramer
Q59109
x-ray crystallography
monomer
-
1* 26800, SDS-PAGE
monomer
-
1 * 23500, SDS-PAGE
monomer
-
1 * 27200, SDS-PAGE
multimer
-
alpha2beta2gammaMdeltaN multimer, 2 * 50000 + 2 * 45000 + m * 11000 + n * 8000
octamer
-
-
octamer
-
8 * 63000, SDS-PAGE
tetramer
Saccharomyces bayanus Hefix, Saccharomyces cerevisiae Johannisberg, Saccharomyces cerevisiae Johannisberg sulfite, Saccharomyces cerevisiae Syrena, Saccharomyces cerevisiae Tokay, Saccharomyces cerevisiae Tokay sulfite
-
alpha2,beta2
-
monomer
Desulfovibrio vulgaris Hildenborough
-
1 * 23500, SDS-PAGE; 1 * 27200, SDS-PAGE
-
additional information
-
sulphite reductase contains a beta-haemoprotein and an alpha-flavoprotein component, the latter composed of 8 alpha-chains including FMN-, NADPH-, and FAD-binding domain
additional information
-
sulphite reductase contains a beta-haemoprotein and an alpha-flavoprotein component, the latter composed of 8 alpha-chains including FMN-, NADPH-, and FAD-binding domain; the holoenzyme has (alpha-beta)8-structure, spectroscopic and titration experiments
additional information
-
overview about alpha-beta subunit structure and ligand binding
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
no modification
-
-
no modification
-
-
no modification
-
-
no modification
Saccharomyces bayanus Hefix
-
-
-
no modification
-
-
no modification
Saccharomyces cerevisiae Johannisberg, Saccharomyces cerevisiae Johannisberg sulfite, Saccharomyces cerevisiae Syrena, Saccharomyces cerevisiae Tokay, Saccharomyces cerevisiae Tokay sulfite
-
-
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
crystallized under exclusion of dioxygen
-
hanging drop vapor diffusion method, using 100 mM sodium citrate (pH 6.5), 20% (w/v) PEG 4000, 0.2 M NaCl, and 5% (v/v) 2-propanol
Q59109
sitting drop vapor diffusion method, using 25% (w/v) PEG 3350, 0.2 M KSCN with 10 mM KCl, 10 mM HEPES, pH 7.4 buffer
-
the crystal structure of DsrAB bound to DsrC is solved at a resolution of 2.1 A
-
the crystal structure of DsrAB bound to DsrC is solved at a resolution of 2.8 A; vapor diffusion method with sitting drops
-
flavoprotein component
-
mutant enzymes N194W and R153S, microseeding and vapor diffusion method, using 12% (w/v) PEG 8000
-
overview structure and the complex binding of substrate sulfite or nitrite by siroheme cofactor
-
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0
-
-
half-life 1 h
25
-
-
half-life 4 h
50
-
-
5 min, 50% loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
0.5 M pyridine stabilizes the purified siroheme component
-
EGTA stabilizes
-
glycol stabilizes and reduces the cold lability at 30% concentration
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-80C, 0.05 M Tris-HCl buffer, pH 7.6, several months
-
-80C, 0.05 M Tris-HCl, 6 months
-
-20C, several months
-
-13.5C, 6 months, no loss of activity
-
-20C, 30% glycerol, loss of 85% activity in 24 h, therefore storage of extracts is impractical
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
purified under strict exclusion of dioxygen in a N2 /H2 (95/5%) atmosphere
-
centrifugation
-
; on a Q-Sepharose fast flow and a Q-Sepharose high performance column
-
cytochromes and a minor flavoprotein present in the sulfite reductase-containing fraction are removed; siroheme component is extracted from the enzyme preparation and further purified
-
DEAE-Toyopearl 650S column chromatography, Sephacryl S200HR gel filtration, Q-Sepharose column chromatography, and HiLoad 26/60 Superdex 200 gel filtration
-
NADPH- and FAD-binding sulfite reductase flavoprotein component, recombinant from Escherichia coli
-
Ni-charged immobilized metal affinity column chromatography, SP Sepharose column chromatography, Q Sepharose column chromatography, and Sephadex S300 gel filtration
-
sulfite reductase haemoprotein component
-
phenyl-Sepharose chromatography, F420-Sepharose chromatography and QAE-Sephadex gel filtration
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
into the vector pCR-XL-TOPO for sequencing
Q0A838 and Q0A837
into the vector pCR-XL-TOPO for sequencing
B8PT92 and B8PT93
functional expression of single copy sir gene in transgenic Arabidopsis thaliana plants, identification of promotor, DNA sequence analysis
-
-
-, O93650 and O93651
from Escherichia coli
-
into the vector pCR-XL-TOPO for sequencing
A1AXC9 and A1AXC8
into the vector pCR-XL-TOPO for sequencing
Candidatus Vesicomyosocius okutanii, Chlorobaculum tepidum, Chlorobium chlorochromatii
-
into the vector pCR-XL-TOPO for sequencing
B8PT99 and B8PTA0
into the vector pCR-XL-TOPO for sequencing
A1BCS1 and A1BCS2
into the vector pCR-XL-TOPO for sequencing
A4SC58 and A4SC59
gene expression in Desulfovibrio hosts using broad-range plasmid pDSK519, 50fold increase to native expression, recombinant and native enzymes are indistiguishable
-
CysG gene, encoding sulfite reductase haemoprotein component, overexpression in Escherichia coli
-
CysJ gene, encoding NADPH- and FAD-binding sulfite reductase flavoprotein component, overexpression in Escherichia coli
-
expressed in Escherichia coli LMG194 cells
-
into the vector pCR-XL-TOPO for sequencing
B8PTB5 and B8PTB6
into the vector pCR-XL-TOPO for sequencing
A1WYF3 and A1WYF4
into the vector pCR-XL-TOPO for sequencing
Magnetococcus sp.
-
into the vector pCR-XL-TOPO for sequencing
A4TYV1 and A4TYV0
into the vector pCR-XL-TOPO for sequencing
Q2W1V4 and Q2W1V3
into the vector pCR-XL-TOPO for sequencing
-
expression in Methanococcus maripaludis at high protein and activity levels, allowing the recombinant strain to carry out F420H2-dependent reduction of sulfite
-
into the vector pCR-XL-TOPO for sequencing
Q3SG18 and Q3SG19
into the vector pCR-XL-TOPO for sequencing
B8PTB3 and B8PTB4
into the vector pCR-XL-TOPO for sequencing
B8PTB0 and B8PTB1
into the vector pCR-XL-TOPO for sequencing
B8PTA5 and B8PTA6
into the vector pCR-XL-TOPO for sequencing
B8PT95 and B8PT96
into the vector pCR-XL-TOPO for sequencing
B8PTA1 and B8PTA2
into the vector pCR-XL-TOPO for sequencing
B8PT94
into the vector pCR-XL-TOPO for sequencing
B8PTA3 and B8PTA4
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
K215S the mutant
-
shows only trace activity
N149W
-
the mutant is approximately twice as active as the wild type enzyme
R153S
-
the mutant shows 60% of wild type activity
R83S
-
the mutant shows 60% of wild type activity
additional information
-
naturally occuring mutant strains with blocks in the assimilatory sulfate reduction pathway
K217S
-
the mutant shows reduced activity
additional information
-
SiR-FP60, N-terminal truncated sulfite reductase flavoprotein component behaves as a monomer and no longer polymerizes to an octamer, but retaines full catalytic activity
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
steel industry
-
enzyme inhibition helps against the corrosion of steel and contamination by excess production of sulfide from sulfate-reducing bacteria
agriculture
-
possible target to minimize H2S production of yeast during wine fermentation