Information on EC 1.8.99.3 - hydrogensulfite reductase

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

EC NUMBER
COMMENTARY
1.8.99.3
-
RECOMMENDED NAME
GeneOntology No.
hydrogensulfite reductase
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S(SO3-)2 + acceptor + 2 H2O + OH- = 3 HSO3- + reduced acceptor
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
reduction
-
reduction of sulfite, thiosulfate, and elemental sulfur, but not of sulfate
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
sulfate reduction V (dissimilatory)
-
-
non-pathway related
-
-
Nitrotoluene degradation
-
-
Sulfur metabolism
-
-
Microbial metabolism in diverse environments
-
-
SYSTEMATIC NAME
IUBMB Comments
trithionate:acceptor oxidoreductase
Methylviologen can act as acceptor. A group of sirohemoproteins containing iron-sulfur centres (P-582).
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
bisulfite reductase
-
-
-
-
bisulfite reductase
-
-
bisulfite reductase (P582)
-
-
-
-
carbon monoxide-binding pigment P582
-
-
desulfofuscidin
-
-
-
-
desulforubidin
-
-
-
-
desulfoviridin
-
-
-
-
desulfoviridin
-
-
dissimilatory (bi)sulfite reductase
-
-
dissimilatory (bi)sulfite reductase
-
dissimilatory (bi)sulfite reductase
-
dissimilatory (bi)sulfite reductase
-
dissimilatory (bi)sulfite reductase
-
dissimilatory (bi)sulfite reductase
-
dissimilatory (bi)sulfite reductase
-
-
dissimilatory (bi)sulfite reductase
-
dissimilatory (bi)sulfite reductase
-
dissimilatory (bi)sulfite reductase
-
-
dissimilatory (bi)sulfite reductase
-
dissimilatory (bi)sulfite reductase
Q69I16 and Q69I15
-
dissimilatory bisulfite reductase
-
dissimilatory sulfite reductase
-
-
-
-
dissimilatory sulfite reductase
-
-
dissimilatory sulfite reductase
-
-
dissimilatory sulfite reductase
-
-
dissimilatory sulfite reductase
-
-
dissimilatory sulfite reductase
-
-
dissimilatory sulfite reductase
-
-
dissimilatory sulfite reductase
-
-
dissimilatory sulfite reductase
-
-
dissimilatory sulfite reductase
Desulfovibrio vulgaris Hildenborough
-
-
-
dissimilatory sulfite reductase
-
dissimilatory sulfite reductase D
-
-
dissimilatory sulphite reductase
-
-
dissimilatory sulphite reductase
Q59110 and Q59109
-
dissimilatory sulphite reductase
-
dissimilatory sulphite reductase
Desulfovibrio gigas ATCC 19364
-
-
dissimilatory-type sulfite reductase
-
-
-
-
Dsr-I
active isoform
Dsr-I
Desulfovibrio gigas ATCC 19364
active isoform
-
Dsr-II
active isoform
Dsr-II
Desulfovibrio gigas ATCC 19364
active isoform
-
Dsr-III
inactive isoform
Dsr-III
Desulfovibrio gigas ATCC 19364
inactive isoform
-
DsrA
Q59110 and Q59109
gene name, subunit alpha
DsrAB
Q69I16 and Q69I15
-
DsrB
Q59110 and Q59109
gene name, subunit beta
reductase, bisulfite
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
42612-25-9
-
85876-01-3
-
9045-15-2
-
9059-42-1
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
renamed Archaeoglobus vinosum
Uniprot
Manually annotated by BRENDA team
Q59110: subunit beta, Q59109: subunit alpha
Q59110 and Q59109
SwissProt
Manually annotated by BRENDA team
-
O93650 and O93651
UniProt
Manually annotated by BRENDA team
dissimilatory sulfite reductase subunit A
EMBL
Manually annotated by BRENDA team
dissimilatory sulfite reductase subunit B
EMBL
Manually annotated by BRENDA team
dissimilatory sulfite reductase subunit A
SwissProt
Manually annotated by BRENDA team
dissimilatory sulfite reductase subunit B
SwissProt
Manually annotated by BRENDA team
RZATAU, desulfoviridin
-
-
Manually annotated by BRENDA team
sulfite reductase, no desulfoviridin
-
-
Manually annotated by BRENDA team
dissimilatory sulfite reductase subunit A
SwissProt
Manually annotated by BRENDA team
dissimilatory sulfite reductase subunit B
SwissProt
Manually annotated by BRENDA team
dissimilatory sulfite reductase subunit A
SwissProt
Manually annotated by BRENDA team
dissimilatory sulfite reductase subunit B
SwissProt
Manually annotated by BRENDA team
dissimilatory sulfite reductase subunit A
SwissProt
Manually annotated by BRENDA team
dissimilatory sulfite reductase subunit B
SwissProt
Manually annotated by BRENDA team
strain DSM 1743, desulforubidin
-
-
Manually annotated by BRENDA team
formerly known as Desulfovibrio desulfuricans strain Norway 4 and Desulfovibrio baculatus strain Norway 4
UniProt
Manually annotated by BRENDA team
strain 5ac10
-
-
Manually annotated by BRENDA team
Desulfonema limicola 5ac10
strain 5ac10
-
-
Manually annotated by BRENDA team
desulforibidin
-
-
Manually annotated by BRENDA team
dissimilatory sulfite reductase subunit A
SwissProt
Manually annotated by BRENDA team
dissimilatory sulfite reductase subunit B
SwissProt
Manually annotated by BRENDA team
Benghazi, NCIB 8401
-
-
Manually annotated by BRENDA team
Desulfovibrio desulfuricans Essex
strain Essex
-
-
Manually annotated by BRENDA team
Desulfovibrio desulfuricans Norway
Norway strain
-
-
Manually annotated by BRENDA team
alpha subunit
UniProt
Manually annotated by BRENDA team
beta subunit
UniProt
Manually annotated by BRENDA team
desulfoviridin
-
-
Manually annotated by BRENDA team
Desulfovibrio gigas ATCC 19364
alpha subunit
UniProt
Manually annotated by BRENDA team
Desulfovibrio gigas ATCC 19364
beta subunit
UniProt
Manually annotated by BRENDA team
strain ThAc01, desulfoviridin
-
-
Manually annotated by BRENDA team
Desulfovibrio sulfodismutans ThAc01
strain ThAc01, desulfoviridin
-
-
Manually annotated by BRENDA team
2 enzyme forms DSF-I and DSF-II
-
-
Manually annotated by BRENDA team
dissimilatory sulfite reductase subunit A
SwissProt
Manually annotated by BRENDA team
dissimilatory sulfite reductase subunit B
SwissProt
Manually annotated by BRENDA team
strain Miyazaki
-
-
Manually annotated by BRENDA team
Desulfovibrio vulgaris Hildenborough
strain Hildenborough
-
-
Manually annotated by BRENDA team
Desulfovibrio vulgaris Miyazaki
strain Miyazaki
-
-
Manually annotated by BRENDA team
Desulfovibrio vulgaris Miyazaki F
Miyazaki F
-
-
Manually annotated by BRENDA team
SUIYOdsr-A gene
SwissProt
Manually annotated by BRENDA team
SUIYOdsr-B gene
SwissProt
Manually annotated by BRENDA team
dissimilatory sulfite reductase subunit A
EMBL
Manually annotated by BRENDA team
dissimilatory sulfite reductase subunit B
EMBL
Manually annotated by BRENDA team
subunit alpha and subunit beta
Q69I16 and Q69I15
UniProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
bisulfite + electron donor
? + oxidized electron donor
show the reaction diagram
-
-
-
?
bisulfite + electron donor
? + oxidized electron donor
show the reaction diagram
-
-
-
-
bisulfite + electron donor
? + oxidized electron donor
show the reaction diagram
-
-
-
-
bisulfite + electron donor
? + oxidized electron donor
show the reaction diagram
-
-
-
-
bisulfite + electron donor
? + oxidized electron donor
show the reaction diagram
-
-
-
-
bisulfite + electron donor
? + oxidized electron donor
show the reaction diagram
-
-
-
?
bisulfite + electron donor
? + oxidized electron donor
show the reaction diagram
-
-
-
-
bisulfite + electron donor
? + oxidized electron donor
show the reaction diagram
-
-
-
?
bisulfite + reduced acceptor
trithionate + acceptor + H2O + OH-
show the reaction diagram
-
-
-
?
bisulfite + reduced acceptor
trithionate + acceptor + H2O + OH-
show the reaction diagram
Q69I16 and Q69I15
-
-
?
hydroxylamine + electron donor
NH3 + H2O + oxidized electron donor
show the reaction diagram
-
-
-
?
hydroxylamine + electron donor
NH3 + H2O + oxidized electron donor
show the reaction diagram
-
-
-
?
hydroxylamine + electron donor
NH3 + H2O + oxidized electron donor
show the reaction diagram
-
-
-
?
hydroxylamine + electron donor
NH3 + H2O + oxidized electron donor
show the reaction diagram
-
-
-
?
hydroxylamine + electron donor
NH3 + H2O + oxidized electron donor
show the reaction diagram
-
-
-
?
hydroxylamine + electron donor
NH3 + H2O + oxidized electron donor
show the reaction diagram
-
electron acceptor: reduced methyl viologen
-
?
nitrite + electron donor
NH3 + H2O + oxidized electron donor
show the reaction diagram
-
-
-
?
nitrite + electron donor
NH3 + H2O + oxidized electron donor
show the reaction diagram
-
-
-
?
nitrite + electron donor
NH3 + H2O + oxidized electron donor
show the reaction diagram
-
-
-
?
nitrite + electron donor
NH3 + H2O + oxidized electron donor
show the reaction diagram
-
-
-
?
nitrite + electron donor
NH3 + H2O + oxidized electron donor
show the reaction diagram
-
electron acceptor: reduced methyl viologen
-
?
nitrite + electron donor
NH3 + H2O + oxidized electron donor
show the reaction diagram
Desulfovibrio vulgaris Hildenborough
-
-
-
?
sulfide + electron acceptor
?
show the reaction diagram
Desulfovibrio desulfuricans, Desulfovibrio desulfuricans Essex
-
electron acceptor: cytochrome c3
-
-
?
sulfide + electron acceptor
? + oxidized electron donor
show the reaction diagram
Desulfovibrio desulfuricans, Desulfovibrio desulfuricans Essex
-
although the bacterium is unable to grow with sulfide as electron donor the dissimilatory sulfite reductase catalyzes the oxidation of sulfide in vivo
-
?
sulfite + electron donor
trithionate + thiosulfate + sulfide + polythionate + oxidized electron donor
show the reaction diagram
-
-
-
?
sulfite + electron donor
trithionate + thiosulfate + sulfide + polythionate + oxidized electron donor
show the reaction diagram
-
-
-
?
sulfite + electron donor
trithionate + thiosulfate + sulfide + polythionate + oxidized electron donor
show the reaction diagram
-
-
-
?
sulfite + electron donor
trithionate + thiosulfate + sulfide + polythionate + oxidized electron donor
show the reaction diagram
-
-
-
?
sulfite + electron donor
trithionate + thiosulfate + sulfide + polythionate + oxidized electron donor
show the reaction diagram
-
-
-
?
sulfite + electron donor
trithionate + thiosulfate + sulfide + polythionate + oxidized electron donor
show the reaction diagram
-
-
-
?
sulfite + electron donor
trithionate + thiosulfate + sulfide + polythionate + oxidized electron donor
show the reaction diagram
-
-
-
?
sulfite + electron donor
trithionate + thiosulfate + sulfide + polythionate + oxidized electron donor
show the reaction diagram
-
-
-
?
sulfite + electron donor
trithionate + thiosulfate + sulfide + polythionate + oxidized electron donor
show the reaction diagram
-
-
-
?
sulfite + electron donor
trithionate + thiosulfate + sulfide + polythionate + oxidized electron donor
show the reaction diagram
-
-
-
?
sulfite + electron donor
trithionate + thiosulfate + sulfide + polythionate + oxidized electron donor
show the reaction diagram
-
-
-
?
sulfite + electron donor
trithionate + thiosulfate + sulfide + polythionate + oxidized electron donor
show the reaction diagram
-
-
-
?
sulfite + electron donor
trithionate + thiosulfate + sulfide + polythionate + oxidized electron donor
show the reaction diagram
-
-
-
?
sulfite + electron donor
trithionate + thiosulfate + sulfide + polythionate + oxidized electron donor
show the reaction diagram
-
-
-
?
sulfite + electron donor
trithionate + thiosulfate + sulfide + polythionate + oxidized electron donor
show the reaction diagram
-
-
-
?
sulfite + electron donor
trithionate + thiosulfate + sulfide + polythionate + oxidized electron donor
show the reaction diagram
-
-
-
?
sulfite + electron donor
trithionate + thiosulfate + sulfide + polythionate + oxidized electron donor
show the reaction diagram
-
-
-
?
sulfite + electron donor
trithionate + thiosulfate + sulfide + polythionate + oxidized electron donor
show the reaction diagram
-
-
-
?
sulfite + electron donor
trithionate + thiosulfate + sulfide + polythionate + oxidized electron donor
show the reaction diagram
-
-
-
?
sulfite + electron donor
trithionate + thiosulfate + sulfide + polythionate + oxidized electron donor
show the reaction diagram
-
-
-
?
sulfite + electron donor
trithionate + thiosulfate + sulfide + polythionate + oxidized electron donor
show the reaction diagram
-
-
-
?
sulfite + electron donor
trithionate + thiosulfate + sulfide + polythionate + oxidized electron donor
show the reaction diagram
-
-
-
?
sulfite + electron donor
trithionate + thiosulfate + sulfide + polythionate + oxidized electron donor
show the reaction diagram
-
-
-
?
sulfite + electron donor
trithionate + thiosulfate + sulfide + polythionate + oxidized electron donor
show the reaction diagram
-
-
-
?
sulfite + electron donor
trithionate + thiosulfate + sulfide + polythionate + oxidized electron donor
show the reaction diagram
-
-
-
?
sulfite + electron donor
trithionate + thiosulfate + sulfide + polythionate + oxidized electron donor
show the reaction diagram
-
-
-
sulfite + electron donor
trithionate + thiosulfate + sulfide + polythionate + oxidized electron donor
show the reaction diagram
-
-
trithionate and thiosulfate as intermediate compounds
?
sulfite + electron donor
trithionate + thiosulfate + sulfide + polythionate + oxidized electron donor
show the reaction diagram
-
-
trithionate and thiosulfate as intermediate compounds
?
sulfite + electron donor
trithionate + thiosulfate + sulfide + polythionate + oxidized electron donor
show the reaction diagram
-
-
enzyme produces mainly trithionate, besides thiosulfate and sulfide
?
sulfite + electron donor
trithionate + thiosulfate + sulfide + polythionate + oxidized electron donor
show the reaction diagram
-
-
enzyme produces mainly trithionate, besides thiosulfate and sulfide
?
sulfite + electron donor
trithionate + thiosulfate + sulfide + polythionate + oxidized electron donor
show the reaction diagram
-
-
trithionate, thiosulfate, tetrathionate and sulfide, variations in assay conditions cause variations in the end product of sulfite reduction
?
sulfite + electron donor
trithionate + thiosulfate + sulfide + polythionate + oxidized electron donor
show the reaction diagram
-
-
the major product trithionate is formed in 5 to 10times higher amounts than thiosulfate and sulfide
?
sulfite + electron donor
trithionate + thiosulfate + sulfide + polythionate + oxidized electron donor
show the reaction diagram
-
electron donor: methyl viologen
-
?
sulfite + electron donor
trithionate + thiosulfate + sulfide + polythionate + oxidized electron donor
show the reaction diagram
-
electron donor: methyl viologen
-
?
sulfite + electron donor
trithionate + thiosulfate + sulfide + polythionate + oxidized electron donor
show the reaction diagram
-
electron donor: methyl viologen
-
?
sulfite + electron donor
trithionate + thiosulfate + sulfide + polythionate + oxidized electron donor
show the reaction diagram
-
electron donor: methyl viologen
-
?
sulfite + electron donor
trithionate + thiosulfate + sulfide + polythionate + oxidized electron donor
show the reaction diagram
-
electron donor: methyl viologen
-
?
sulfite + electron donor
trithionate + thiosulfate + sulfide + polythionate + oxidized electron donor
show the reaction diagram
-
electron donor: methyl viologen
-
?
sulfite + electron donor
trithionate + thiosulfate + sulfide + polythionate + oxidized electron donor
show the reaction diagram
-
electron donor: methyl viologen
-
?
sulfite + electron donor
trithionate + thiosulfate + sulfide + polythionate + oxidized electron donor
show the reaction diagram
-
electron donor: methyl viologen
-
?
sulfite + electron donor
trithionate + thiosulfate + sulfide + polythionate + oxidized electron donor
show the reaction diagram
-
electron donor: methyl viologen
-
?
sulfite + electron donor
trithionate + thiosulfate + sulfide + polythionate + oxidized electron donor
show the reaction diagram
-
electron donor: methyl viologen
forms mainly trithionate besides thiosulfate and sulfide in sulfite reduction coupled to hydrogenase and methyl viologen
?
sulfite + electron donor
trithionate + thiosulfate + sulfide + polythionate + oxidized electron donor
show the reaction diagram
-
electron donor: methyl viologen
with reduced methyl viologen as electron donor, the major product of sulfite reduction is trithionate
?
sulfite + electron donor
trithionate + thiosulfate + sulfide + polythionate + oxidized electron donor
show the reaction diagram
-
electron donor: methyl viologen
formation of trithionate, thiosulfate and sulfide when coupled with a hydrogenase-methyl viologen system
?
sulfite + electron donor
trithionate + thiosulfate + sulfide + polythionate + oxidized electron donor
show the reaction diagram
-
electron donor: methyl viologen
enzyme produces mainly trithionate, besides thiosulfate and sulfide
?
sulfite + electron donor
trithionate + thiosulfate + sulfide + polythionate + oxidized electron donor
show the reaction diagram
-
electron donor: methyl viologen
enzyme produces mainly trithionate, besides thiosulfate and sulfide
?
sulfite + electron donor
trithionate + thiosulfate + sulfide + polythionate + oxidized electron donor
show the reaction diagram
-
electron donor: methyl viologen
sulfide, thiosulfate and trithionate
?
sulfite + electron donor
trithionate + thiosulfate + sulfide + polythionate + oxidized electron donor
show the reaction diagram
-
electron donor: cytochrome c3
-
?
sulfite + electron donor
trithionate + thiosulfate + sulfide + polythionate + oxidized electron donor
show the reaction diagram
-
electron donor: cytochrome c3
-
?
sulfite + electron donor
trithionate + thiosulfate + sulfide + polythionate + oxidized electron donor
show the reaction diagram
-
electron donor: cytochrome c3
-
?
sulfite + electron donor
trithionate + thiosulfate + sulfide + polythionate + oxidized electron donor
show the reaction diagram
-
electron donor: benzyl viologen
with reduced methyl viologen as electron donor, the major product of sulfite reduction is trithionate
?
sulfite + electron donor
trithionate + thiosulfate + sulfide + polythionate + oxidized electron donor
show the reaction diagram
-
electron donor: benzyl viologen
enzyme produces mainly trithionate, besides thiosulfate and sulfide
?
sulfite + electron donor
trithionate + thiosulfate + sulfide + polythionate + oxidized electron donor
show the reaction diagram
-
electron donor: reduced viologen dyes
sulfide, thiosulfate and trithionate
?
sulfite + electron donor
trithionate + thiosulfate + sulfide + polythionate + oxidized electron donor
show the reaction diagram
Desulfovibrio sulfodismutans ThAc01
-
-
-
?
sulfite + electron donor
trithionate + thiosulfate + sulfide + polythionate + oxidized electron donor
show the reaction diagram
Desulfovibrio desulfuricans Essex
-
electron donor: cytochrome c3
-
?
sulfite + electron donor
trithionate + thiosulfate + sulfide + polythionate + oxidized electron donor
show the reaction diagram
Desulfovibrio desulfuricans Essex
-
-
-
?
sulfite + electron donor
trithionate + thiosulfate + sulfide + polythionate + oxidized electron donor
show the reaction diagram
Desulfovibrio vulgaris Miyazaki
-
-
-
?
sulfite + electron donor
trithionate + thiosulfate + sulfide + polythionate + oxidized electron donor
show the reaction diagram
Desulfovibrio vulgaris Miyazaki F
-
electron donor: methyl viologen
formation of trithionate, thiosulfate and sulfide when coupled with a hydrogenase-methyl viologen system
?
sulfite + electron donor
trithionate + thiosulfate + sulfide + polythionate + oxidized electron donor
show the reaction diagram
Desulfonema limicola 5ac10
-
-
-
?
sulfite + electron donor
trithionate + thiosulfate + sulfide + polythionate + oxidized electron donor
show the reaction diagram
Desulfovibrio vulgaris Hildenborough
-
-
-
?
sulfite + electron donor
trithionate + thiosulfate + sulfide + polythionate + oxidized electron donor
show the reaction diagram
Desulfovibrio vulgaris Hildenborough
-
-
-
?
sulfite + electron donor
trithionate + thiosulfate + sulfide + polythionate + oxidized electron donor
show the reaction diagram
Desulfovibrio vulgaris Hildenborough
-
-
-
?
sulfite + electron donor
trithionate + thiosulfate + sulfide + polythionate + oxidized electron donor
show the reaction diagram
Desulfovibrio vulgaris Hildenborough
-
-
-
?
sulfite + electron donor
trithionate + thiosulfate + sulfide + polythionate + oxidized electron donor
show the reaction diagram
Desulfovibrio vulgaris Hildenborough
-
-
-
?
sulfite + electron donor
trithionate + thiosulfate + sulfide + polythionate + oxidized electron donor
show the reaction diagram
Desulfovibrio desulfuricans Norway
-
electron donor: methyl viologen
-
?
sulfite + electron donor
? + oxidized electron donor
show the reaction diagram
-
-
-
?
sulfite + electron donor
? + oxidized electron donor
show the reaction diagram
-
reduction of bisulfite to sulfide by a dissimilatory pathway involving trithionate and thiosulfate as intermediate
-
?
sulfite + electron donor
? + oxidized electron donor
show the reaction diagram
-
enzyme is involved in energy conservation by reducing sulfite, which is formed during the degradation of taurine as an electron acceptor to sulfide
-
?
sulfite + electron donor
? + oxidized electron donor
show the reaction diagram
-
dissimilatory reduction of sulfite or disulfite
-
?
sulfite + electron donor
? + oxidized electron donor
show the reaction diagram
-
dissimilatory reduction of sulfite or disulfite
-
?
sulfite + electron donor
? + oxidized electron donor
show the reaction diagram
-
dissimilatory reduction of sulfite or disulfite
-
?
sulfite + electron donor
? + oxidized electron donor
show the reaction diagram
-
dissimilatory reduction of sulfite or disulfite
-
?
sulfite + electron donor
? + oxidized electron donor
show the reaction diagram
-
dissimilatory reduction of sulfite or disulfite
-
?
sulfite + electron donor
? + oxidized electron donor
show the reaction diagram
-
dissimilatory reduction of sulfite or disulfite
-
?
sulfite + electron donor
? + oxidized electron donor
show the reaction diagram
-
dissimilatory reduction of sulfite or disulfite
-
?
sulfite + electron donor
? + oxidized electron donor
show the reaction diagram
-
dissimilatory reduction of sulfite or disulfite
-
?
sulfite + electron donor
? + oxidized electron donor
show the reaction diagram
-
dissimilatory reduction of sulfite or disulfite
-
?
sulfite + electron donor
? + oxidized electron donor
show the reaction diagram
-
dissimilatory reduction of sulfite or disulfite
-
?
sulfite + electron donor
? + oxidized electron donor
show the reaction diagram
-
dissimilatory reduction of sulfite or disulfite
-
?
sulfite + electron donor
? + oxidized electron donor
show the reaction diagram
-
dissimilatory reduction of sulfite or disulfite
-
?
sulfite + electron donor
? + oxidized electron donor
show the reaction diagram
-
dissimilatory reduction of sulfite or disulfite
-
?
sulfite + electron donor
? + oxidized electron donor
show the reaction diagram
Desulfovibrio desulfuricans Essex
-
dissimilatory reduction of sulfite or disulfite
-
?
sulfite + electron donor
? + oxidized electron donor
show the reaction diagram
Desulfovibrio desulfuricans Essex
-
dissimilatory reduction of sulfite or disulfite
-
?
sulfite + electron donor
? + oxidized electron donor
show the reaction diagram
Desulfonema limicola 5ac10
-
dissimilatory reduction of sulfite or disulfite
-
?
sulfite + electron donor
? + oxidized electron donor
show the reaction diagram
Desulfovibrio vulgaris Hildenborough
-
dissimilatory reduction of sulfite or disulfite
-
?
sulfite + electron donor
? + oxidized electron donor
show the reaction diagram
Desulfovibrio vulgaris Hildenborough
-
dissimilatory reduction of sulfite or disulfite
-
?
sulfite + methyl viologen
trithionate + thiosulfate + sulfide + oxidized methyl viologen
show the reaction diagram
-
-
?
sulfite + methyl viologen
trithionate + thiosulfate + sulfide + oxidized methyl viologen
show the reaction diagram
Desulfovibrio gigas ATCC 19364
-
-
?
sulfite + reduced ferredoxin-I
trithionate + ferredoxin-I + H2O + OH-
show the reaction diagram
-
-
?
sulfite + reduced pyruvate-ferredoxin oxidoreductase
trithionate + pyruvate-ferredoxin oxidoreductase + H2O + OH-
show the reaction diagram
-
-
?
thiosulfate + electron donor
sulfate + sulfur + oxidized electron donor
show the reaction diagram
-
-
-
?
trimethylamine N-oxide + electron donor
? + oxidized electron donor
show the reaction diagram
-
-
-
?
hydroxylamine + electron donor
NH3 + H2O + oxidized electron donor
show the reaction diagram
Desulfovibrio vulgaris Hildenborough
-
-
-
?
additional information
?
-
-
catalyzes the formation of sulfide from sulfite
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
bisulfite + reduced acceptor
trithionate + acceptor + H2O + OH-
show the reaction diagram
-
-
-
?
sulfide + electron acceptor
? + oxidized electron donor
show the reaction diagram
Desulfovibrio desulfuricans, Desulfovibrio desulfuricans Essex
-
although the bacterium is unable to grow with sulfide as electron donor the dissimilatory sulfite reductase catalyzes the oxidation of sulfide in vivo
-
?
sulfite + electron donor
trithionate + thiosulfate + sulfide + polythionate + oxidized electron donor
show the reaction diagram
Q93UT1
-
-
-
sulfite + electron donor
? + oxidized electron donor
show the reaction diagram
-
reduction of bisulfite to sulfide by a dissimilatory pathway involving trithionate and thiosulfate as intermediate
-
?
sulfite + electron donor
? + oxidized electron donor
show the reaction diagram
-
enzyme is involved in energy conservation by reducing sulfite, which is formed during the degradation of taurine as an electron acceptor to sulfide
-
?
sulfite + electron donor
? + oxidized electron donor
show the reaction diagram
-
dissimilatory reduction of sulfite or disulfite
-
?
sulfite + electron donor
? + oxidized electron donor
show the reaction diagram
-
dissimilatory reduction of sulfite or disulfite
-
?
sulfite + electron donor
? + oxidized electron donor
show the reaction diagram
-
dissimilatory reduction of sulfite or disulfite
-
?
sulfite + electron donor
? + oxidized electron donor
show the reaction diagram
-
dissimilatory reduction of sulfite or disulfite
-
?
sulfite + electron donor
? + oxidized electron donor
show the reaction diagram
-
dissimilatory reduction of sulfite or disulfite
-
?
sulfite + electron donor
? + oxidized electron donor
show the reaction diagram
-
dissimilatory reduction of sulfite or disulfite
-
?
sulfite + electron donor
? + oxidized electron donor
show the reaction diagram
-
dissimilatory reduction of sulfite or disulfite
-
?
sulfite + electron donor
? + oxidized electron donor
show the reaction diagram
-
dissimilatory reduction of sulfite or disulfite
-
?
sulfite + electron donor
? + oxidized electron donor
show the reaction diagram
-
dissimilatory reduction of sulfite or disulfite
-
?
sulfite + electron donor
? + oxidized electron donor
show the reaction diagram
-
dissimilatory reduction of sulfite or disulfite
-
?
sulfite + electron donor
? + oxidized electron donor
show the reaction diagram
-
dissimilatory reduction of sulfite or disulfite
-
?
sulfite + electron donor
? + oxidized electron donor
show the reaction diagram
-
dissimilatory reduction of sulfite or disulfite
-
?
sulfite + electron donor
? + oxidized electron donor
show the reaction diagram
-
dissimilatory reduction of sulfite or disulfite
-
?
sulfite + electron donor
? + oxidized electron donor
show the reaction diagram
Desulfovibrio desulfuricans Essex
-
dissimilatory reduction of sulfite or disulfite
-
?
sulfite + electron donor
? + oxidized electron donor
show the reaction diagram
Desulfovibrio desulfuricans Essex
-
dissimilatory reduction of sulfite or disulfite
-
?
sulfite + electron donor
? + oxidized electron donor
show the reaction diagram
Desulfonema limicola 5ac10
-
dissimilatory reduction of sulfite or disulfite
-
?
sulfite + electron donor
? + oxidized electron donor
show the reaction diagram
Desulfovibrio vulgaris Hildenborough
-
dissimilatory reduction of sulfite or disulfite
-
?
sulfite + electron donor
? + oxidized electron donor
show the reaction diagram
Desulfovibrio vulgaris Hildenborough
-
dissimilatory reduction of sulfite or disulfite
-
?
bisulfite + reduced acceptor
trithionate + acceptor + H2O + OH-
show the reaction diagram
Q69I16 and Q69I15
-
-
?
additional information
?
-
-
catalyzes the formation of sulfide from sulfite
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(7S,8S,12S,13S)-3,8,13,17-tetrakis(carboxymethyl)-8,13-dimethyl-7,8,12,13-tetrahydroporphyrin-2,7,12,18-tetrapropionic acid
isoforms Dsr-I and DsrII contain two flat sirohydrochlorins; isoforms Dsr-I and DsrII contain two flat sirohydrochlorins
Ferredoxin
the C-terminal region defines the ferredoxin-binding domain
-
Ferredoxin
-
the C-terminal region defines the ferredoxin-binding domain
-
Ferredoxin
the C-terminal region defines the ferredoxin-binding domain
-
Ferredoxin
-
the C-terminal region defines the ferredoxin-binding domain
-
heme
Q59110 and Q59109
only the alpha subunit binds a siroheme-[4Fe-4S] complex. Chemical analyses shows the presence of only two sirohemes per alpha2beta2 enzyme molecule
siroheme
the siroheme-binding motif occurs near the N-terminus
siroheme
-
the siroheme-binding motif occurs near the N-terminus
siroheme
the siroheme-binding motif occurs near the N-terminus
siroheme
-
the siroheme-binding motif occurs near the N-terminus
siroheme
isoforms Dsr-I and DsrII contain two saddle-shaped sirohemes; isoforms Dsr-I and DsrII contain two saddle-shaped sirohemes
siroheme
contains four sirohemes
[3Fe-4S]-center
isoform Dsr-II contains a [3Fe-4S] cluster in addition to the [4Fe-4S] cluster; isoform Dsr-II contains a [3Fe-4S] cluster in addition to the [4Fe-4S] cluster
[4Fe-4S]-center
isoform Dsr-I and DsrII contain eight [4Fe-4S] clusters, isoform Dsr-II cont; isoform Dsr-I and DsrII contain eight [4Fe-4S] clusters, isoform Dsr-II cont
[4Fe-4S]-center
contains eight [4Fe-4S] clusters
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Iron
-
tetrahydroporphyrin-based prosthetic group sirohydrochlorin
Iron
-
contains two fully metalated sirohemes and Fe-S clusters, 15 Fe and 19 S2-
Iron
-
enzyme contains 4 sirohemes and 8 [4Fe-4S] centers per mol of protein
Iron
-
contains exchange-coupled siroheme-[4Fe-4S] units
Iron
-
iron is the only significant chelatable metal contained in the chromophore sirohydrochlorin
Iron
-
contains siroheme as prosthetic group, 20-21 iron atoms per molecule of protein, native protein contains 4 sirohemes and 4 [4Fe-4S] cluster per molecule
Iron
-
contains siroheme, 24 Fe per enzyme molecule
Iron
-
enzyme form DSF-I contains 0.125 mM of Fe per g of protein, enzyme form DSF-II contains 0.116 mM of Fe per g of protein
Iron
-
contains 51 Fe atoms per enzyme molecule; enzyme contains siroheme
Iron
-
enzyme contains sirohem and Fe-S clusters, reaction of reductase with reduced methyl viologen results in reduction of only the siroheme
Iron
-
enzyme contains siroheme and Fe-S centres in the active site
Iron
-
contains 24 Fe and 18 S2- per 200000 Da enzyme, 5% of the siroheme moiety is metallated
Iron
-
characterization of the redox thermodynamics of the Fe4S4-siroheme prosthetic center
Iron
-
two pairs of [Fe4S4] centers and siroheme units
Iron
-
20 iron atoms per molecule; 4 mol of siroheme per mol of enzyme
Iron
-
32 iron atoms per molecule; 4 mol of siroheme per mol of enzyme
Iron
-
contains 4 [4Fe-4S] clusters, each high-spin ferric siroheme is exchange coupled to a [4Fe-4S]2- cluster, a solitary iron center is not associated with either the sirohemes or [4Fe-4S] clusters
Iron
Q59110 and Q59109
only the alpha subunit binds a sirohaem-[4Fe-4S] complex. Chemical analyses shows the presence of only two sirohemes per alpha2beta2 enzyme molecule and the presence of six [4Fe-4S] clusters per alpha2beta2 enzyme molecule, two of which would be expected to be associated with siroheme while the other four could bind to the ferredoxin-like sites
[4Fe-4S]-center
Q59110 and Q59109
only the alpha subunit binds a sirohaem-[4Fe-4S] complex. Chemical analyses shows the presence of only two sirohemes per alpha2beta2 enzyme molecule and the presence of six [4Fe-4S] clusters per alpha2beta2 enzyme molecule, two of which would be expected to be associated with siroheme while the other four could bind to the ferredoxin-like sites
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
arsenite
-
10 mM, 68% inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cyanide
-
1 mM, slight activation
additional information
-
active form of enzyme binds and catalyzes substrate reduction, inactive enzyme form exists in resting cells
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
48
hydroxylamine
-
-
0.028
nitrite
-
-
0.06
sulfite
-
-
3.6
sulfite
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
Thiobacillus denitrificans
-
-
-
additional information
additional information
Allochromatium vinosum
-
-
-
additional information
additional information
Desulfovibrio vulgaris
-
18.6 mol SO32- * min-1 * mol heme-1, 2.28 mol nitrite * min-1 * mol heme-1, 1740 mol hydroxylamine * min-1 * mol heme-1
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.041
-
soluble enzyme
0.128
-
membranous enzyme
240
-
mutant DELTAdsrJ
additional information
-
-
additional information
-
-
additional information
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 6.5
-
pH 5.0: about 70% of maximal activity, pH 6.5: about 60% of maximal activity, reduction of sulfite
6 - 8
-
pH 6.0: about 50% of maximal activity, pH 8.0: about 90% of maximal activity, reduction of hydroxylamine
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
85
Q59110 and Q59109
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35 - 70
-
35C: very low activity below 35C, 65-70C: maximal activity at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.2
Q59110 and Q59109
analytical isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
activity is highest in sulfite-grown cells
Manually annotated by BRENDA team
Desulfovibrio vulgaris Miyazaki
-
activity is highest in sulfite-grown cells
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Desulfovibrio vulgaris Hildenborough
-
-
-
Manually annotated by BRENDA team
-
two putative transmembrane alpha-helices are postulated on each beta-subunit
Manually annotated by BRENDA team
Desulfovibrio desulfuricans Essex
-
two putative transmembrane alpha-helices are postulated on each beta-subunit
-
Manually annotated by BRENDA team
Desulfovibrio desulfuricans Essex
-
-
-
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Desulfomicrobium norvegicum (strain DSM 1741 / NCIMB 8310)
Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / NCIMB 8303)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
26650
-
gel filtration
673621
42500
DsrB, SDS-PAGE
674238
49900
DsrA, SDS-PAGE
674238
160000
-
gel filtration
394045
167000
-
equilibrium sedimentation
394043, 394069
175000
-
gel filtration
394035
178200
Q59110 and Q59109
-
725630
180000
-
gel filtration
394041
180000
-
disc electrophoresis
394049
190000
-
equilibrium sedimentation
394035
200000
-
gel filtration
392979
200000
-
gel filtration
394046
200000
-
equilibrium sedimentation
394060
200000
-
gel filtration
394066
215100
gel filtration
725077
280000
-
gel filtration
394047
285000
-
gel filtration
394064
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
alpha2beta2gamman, 2 * 49000 + 2 * 54000 + x * 11000, SDS-PAGE
?
-
alpha2beta2gamman, 2 * 500000 + 2 * 450000 + x * 11000, SDS-PAGE
?
Desulfovibrio desulfuricans Essex
-
alpha2beta2gamman, 2 * 500000 + 2 * 450000 + x * 11000, SDS-PAGE
-
dimer
-
2 * 13327, gel filtration
heterodimer
1 * 47000 + 1 * 41000
heterodimer
1 * 47000 + 1 * 41000
heterohexamer
x-ray crystallography
hexamer
-
alpha2beta2gamma2, 2 * 50000 + 2 * 42500 + 2 * 12000, SDS-PAGE
tetramer
-
4 * 44000-48000, SDS-PAGE
tetramer
-
alpha2beta2, 2 * 50000 + 2 * 39000, SDS-PAGE
tetramer
-
alpha2beta2, x * 48000, SDS-PAGE
tetramer
-
alpha2beta2, 2 * 38000 + 2 * 43000, SDS-PAGE
tetramer
-
alpha2beta2, 2 * 37000 + 2 * 42000, SDS-PAGE
tetramer
-
x * 42000 + x * 500000, SDS-PAGE
tetramer
-
2 * 45000 + 2 * 55000, SDS-PAGE
tetramer
-
x * 48000, four similar but not identical subunits, SDS-PAGE
tetramer
Q59110 and Q59109
2 * 40000 + 2 * 50000, alpha2beta2, calculated from sequence; 2 * 41700 + 2 *47400, alpha2beta2, calculated from sequence
tetramer
Desulfovibrio vulgaris Miyazaki F
-
alpha2beta2, 2 * 50000 + 2 * 39000, SDS-PAGE
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapour diffusion method
-
bound to two DsrC proteins, hanging drop vapor diffusion method, using 20% (w/v) PEG 3350, 0.1 M Bis-Tris propane pH 7.5, and 0.2 M K/Na tartrate
hanging drop vapor diffusion method, using PEG6000 (23% (w/v) for isoform Dsr-I and 25% (w/v) for isoform Dsr-II) and sodium chloride (200 mM) in MES buffer (100 mM) at pH 5.5; hanging drop vapor diffusion method, using PEG6000 (23% (w/v) for isoform Dsr-I and 25% (w/v) for isoform Dsr-II) and sodium chloride (200 mM) in MES buffer (100 mM) at pH 5.5
crystal structure determined at 1.2 by the single isomorphous replacement method
-
large crystals, obtained by the sitting-drop vapour-diffussion method followed by macroseeding, are used for a neutron diffraction experiment
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
70
-
stable to, rapidly denatured above
394043
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 1 month, no loss of activity
-
4C, 1 month, 60% loss of activity
-
-20C, 6 months, stable
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
MonoQ HR 5/5 column chromatography
-
-
Q59110 and Q59109
Q-Sepharose Hi-Load column chromatography
-
DEAE-Sepharose column chromatography, Q-Sepharose column chromatography, Mono Q column chromatography, and Sephacryl S-200 gel filtration
DE52 ion exchange column chromatography, Mono Q column chromatography, and Superdex-200 gel filtration; DE52 ion exchange column chromatography, Mono Q column chromatography, and Superdex-200 gel filtration
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
-
Q59110 and Q59109
expressed in Escherichia coli
-
expressed in Escherichia coli
-
into the pCR2.1-TOPO plasmid vector for transformation into Escherichia coli TOP10 cells
-
expressed in Escherichia coli
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
DELTAdsrJ
-
mutant with in frame deletion, unable to oxidize stored sulfur
DELTAdsrK
-
mutant with in frame deletion, unable to oxidize stored sulfur
DELTAdsrL
-
in frame deletion mutant, that is indispensable for sulfur oxidation
DELTAdsrM
-
mutant with in frame deletion, unable to oxidize stored sulfur
DELTAdsrN
-
in frame deletion mutants, sulfur oxidation rate is reduced to 15% of the oxidation rate of the wild type enzyme
DELTAdsrO
-
mutant with in frame deletion, unable to oxidize stored sulfur
DELTAdsrP
-
mutant with in frame deletion, unable to oxidize stored sulfur
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
industry
-
quick detection and accurate quantification of sulfate-reducing bacteria in oil fields are crucial for the design of a process to prevent H2S from being formed and to control reservoir souring