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Enzyme Nomenclature
Information on EC 1.8.1.19 - sulfide dehydrogenase
Word Map on EC 1.8.1.19
- 1.8.1.19
- sulfur
- flavoproteins
- furiosus
-
iron-sulfur
-
flavocytochrome
-
phototrophic
- cyanide
- thiosulfate
-
wolinella
-
sulfide-dependent
-
sulfide-quinone
-
purple
- chromatium
-
sulfur-oxidizing
- succinogenes
- vinosum
-
fad-binding
-
senescence-associated
- h2s
- tepidum
-
autotroph
-
paracoccus
- radish
- chlorobium
-
dark-induced
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The expected taxonomic range for this enzyme is: Pyrococcus furiosus
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EC NUMBER 
COMMENTARY 
1.8.1.19
-
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RECOMMENDED NAME
GeneOntology No.
sulfide dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hydrogen sulfide + (sulfide)n + NADP+ = (sulfide)n+1 + NADPH + H+
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-
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SYSTEMATIC NAME
IUBMB Comments
hydrogen sulfide,polysulfide(n-1):NADP+ oxidoreductase
A iron-sulfur flavoprotein. In the archaeon Pyrococcus furiosus the enzyme is involved in the oxidation of NADPH which is produced in peptide degradation. The enzyme also catalyses the reduction of sulfur with lower activity.
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Q8U195: subunit alpha, and Q8U194: subunit beta
Q8U195 and Q8U194
SwissProt
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
NADPH-dependent S0 reduction by SuDH I and SuDH II may be a mechanism to compensate for the reduction of S0 in the absence of NADPH:sulfur oxidoreductase (NSR)
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(sulfide)n+1 + NADPH + H+
hydrogen sulfide + (sulfide)n + NADP+
Q8U195 and Q8U194
NADH is not utilized as an electron donor for polysulfide reduction. Polysulfide reduction is catalyzed with reduced ferredoxin as an electron donor. However, the rate of sulfide production, at least in vitro, is much lower than when the enzyme uses NADPH to provide reductant for polysulfide reduction
-
-
?
colloidal sulfur + NADPH + H+
?
Q8U195 and Q8U194
the relative activity is about 40% compared to the activity with polysulfide
-
-
?
additional information
?
-
Q8U195 and Q8U194
the enzyme also catalyzes ferredoxin:NADP+ reductase activity
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-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(sulfide)n+1 + NADPH + H+
hydrogen sulfide + (sulfide)n + NADP+
Q8U195 and Q8U194
NADH is not utilized as an electron donor for polysulfide reduction. Polysulfide reduction is catalyzed with reduced ferredoxin as an electron donor. However, the rate of sulfide production, at least in vitro, is much lower than when the enzyme uses NADPH to provide reductant for polysulfide reduction
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-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Fe-S center
-
the enzyme contains approximately four iron-sulfur centers, 11 iron and 6 acid-labile sulfide atoms per mol
Fe-S center
-
the alpha-subunit carries a [2Fe-2S]2+,+ prosthetic group. It exhibits EPR g-values, 2.035, 1.908, 1.786, and reduction potential, Em,8 = +80 mV, reminiscent of Rieske-type clusters. Comparative sequence analysis indicates that this cluster is coordinated by a novel motif of one Asp and three Cys ligands. The beta-subunit carries a [3Fe-4S]+,0 cluster, and a [4Fe-4S]2+,+ cluster. The 3Fe cluster has an unusually high reduction potential, Em,8 = +230 mV. The reduced 4Fe cluster exhibits a complex EPR signal, presumably resulting from magnetic interaction of its S = 1/2 spin with the S=2 spin of the reduced 3Fe cluster. The 4Fe cluster can be reduced with deazaflavin/EDTA/light but not with sodium dithionite, however, it is readily reduced with NADPH
NADPH
-
NADH was not utilized as an electron donor for polysulfide reduction
NADPH
-
both the alpha-subunit and the beta-subunit carry one putative nucleotide binding site for NADPH
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30686
-
1 * 52598 (alpha-subunit, SudA) + 1 * 30686 (beta-subunit, SudB), calculated from sequence
52598
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1 * 52598 (alpha-subunit, SudA) + 1 * 30686 (beta-subunit, SudB), calculated from sequence
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterodimer
heterodimer
-
1 * 52598 (alpha-subunit, SudA) + 1 * 30686 (beta-subunit, SudB), calculated from sequence
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
following sulfur (S0) addition in deletion mutant MBX1 (deletion in membrane-bound oxidoreductase complex, MBX) the expression of the gene encoding sulfide dehydrogenase SuDH I (sudB) is increased 2fold, campared to 10fold increase in the parent strain
following sulfur (S0) addition in deletion mutant NSR1 (deletion in NADPH:sulfur oxidoreductase, NSR) the expression of the gene encoding sulfide dehydrogenase SuDH I (sudB) is decreased to a lesser extent (5fold less) compared to the parent strain
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LINKS TO OTHER DATABASES (specific for EC-Number 1.8.1.19)
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