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Information on EC 1.8.1.22 - dissimilatory sulfite reductase system
for references in articles please use BRENDA:EC1.8.1.22
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EC Tree 1 Oxidoreductases
1.8 Acting on a sulfur group of donors
1.8.1 With NAD+ or NADP+ as acceptor
1.8.1.22 dissimilatory sulfite reductase system
IUBMB Comments
Contains siroheme. The enzyme is essential in prokaryotic sulfur-based energy metabolism, including sulfate/sulfite reducing organisms, sulfur-oxidizing bacteria, and organosulfonate reducers. The system comprises the DsrAB reductase and the DsrL protein, which form a tight complex. The reaction involves the small protein DsrC, which is present in all the organisms that contain dissimilatory sulfite reductase. In sulfite reducers the DsrL component transfers two electrons from NADH to the DsrAB component, which then reduces the sulfur in sulfite to an S(II) intermediate that forms (together with two cysteine residues of DsrC) a trisulfide. In sulfur oxidizers the enzyme catalyses the opposite reaction .
The enzyme appears in viruses and cellular organisms
Reaction Schemes
showa [DsrC protein]-trisulfide
+
+
3
=
a [DsrC protein]-dithiol
+
+
+
+
3
+
3
=
+
+
3
+
2
a [DsrC protein]-S-sulfanyl-L-cysteine
+
3
+
3
=
+
a [DsrC protein]-disulfide
+
3
+
2
Synonyms
bisulfite reductase, CNL05500, desulforubidin, desulfoviridin, desulphoviridin, dissimilatory sulfite reductase, dissimilatory sulphite reductase, dissimilatory-type sulfite reductase, dSiR, DSR, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
bisulfite reductase
CNL05500
desulforubidin
desulfoviridin
desulphoviridin
dissimilatory sulfite reductase
dissimilatory sulphite reductase
dSiR
DsrA
DsrAB
DsrAB-type dissimilatory (bi)sulfite reductase
DsrC
DsvA
DsvB
hydrogen-sulfide:(acceptor) oxidoreductase
-
-
ambiguous
-
low-spin sulfite reductase
MET5
mSIR
PAE2566
rDSR
reverse dissimilatory sulfite reductase
reversely operating sirohaem dissimilatory sulfite reductase
siroheme sulfite reductase
-
-
-
-
sulfite reductase
desulphoviridin
Megalodesulfovibrio gigas No. 9332
-
-
-
dissimilatory sulfite reductase
-
dissimilatory sulfite reductase
-
dissimilatory sulfite reductase
-
dissimilatory sulfite reductase
-
dissimilatory sulfite reductase
-
dissimilatory sulfite reductase
Q2M446; Q2M447, Q2M449; Q2M448, Q2M451; Q2M450, Q2M453; Q2M452, Q2M455; Q2M454, Q2M456; Q2M457, Q2M459; Q2M458, Q2M460; Q2M461, Q2M463; Q2M462, Q2M464; Q2M465, Q2M466; Q2M467, Q2M468; Q2M469, Q2M471; Q2M470, Q2M472; Q2M473, Q2M475; Q2M474, Q2M476; Q2M477, Q2M479; Q2M478, Q2M481; Q2M480, Q2M483; Q2M482, Q2M485; Q2M484, Q2M487; Q2M486
-
dissimilatory sulphite reductase
Megalodesulfovibrio gigas No. 9332
-
-
-
DsrA
-
alpha subunit of dissimilatory sulfite reductase
-
DsrA
Nitratidesulfovibrio vulgaris Hildenborough
-
alpha subunit of dissimilatory sulfite reductase
-
DsrAB
-
-
ambiguous
-
DsrAB
-
DsrAB
Q2M446; Q2M447, Q2M449; Q2M448, Q2M451; Q2M450, Q2M453; Q2M452, Q2M455; Q2M454, Q2M456; Q2M457, Q2M459; Q2M458, Q2M460; Q2M461, Q2M463; Q2M462, Q2M464; Q2M465, Q2M466; Q2M467, Q2M468; Q2M469, Q2M471; Q2M470, Q2M472; Q2M473, Q2M475; Q2M474, Q2M476; Q2M477, Q2M479; Q2M478, Q2M481; Q2M480, Q2M483; Q2M482, Q2M485; Q2M484, Q2M487; Q2M486
-
DsrAB-type dissimilatory (bi)sulfite reductase
-
DsrAB-type dissimilatory (bi)sulfite reductase
Thioalkalivibrio thiocyanodenitrificans DSM 16954
-
-
-
reversely operating sirohaem dissimilatory sulfite reductase
-
-
reversely operating sirohaem dissimilatory sulfite reductase
-
-
-
reversely operating sirohaem dissimilatory sulfite reductase
-
-
reversely operating sirohaem dissimilatory sulfite reductase
-
-
-
reversely operating sirohaem dissimilatory sulfite reductase
-
-
-
reversely operating sirohaem dissimilatory sulfite reductase
-
-
reversely operating sirohaem dissimilatory sulfite reductase
-
-
-
reversely operating sirohaem dissimilatory sulfite reductase
-
-
-
reversely operating sirohaem dissimilatory sulfite reductase
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a [DsrC protein]-S-sulfanyl-L-cysteine + 2 acceptor + 3 H2O = sulfite + a [DsrC protein]-dithiol + 2 reduced acceptor + 2 H+
(1b)
-
-
-
a [DsrC protein]-S-sulfanyl-L-cysteine + 3 acceptor + 3 H2O = a [DsrC]-S-sulfo-L-cysteine + 3 reduced acceptor + H+
(2a)
-
-
-
a [DsrC protein]-S-sulfanyl-L-cysteine + 3 acceptor + 3 H2O = sulfite + a [DsrC protein]-disulfide + 3 reduced acceptor + 2 H+
(2), overall reaction
-
-
-
a [DsrC protein]-trisulfide + NAD+ + 3 H2O = a [DsrC protein]-dithiol + sulfite + NADH + H+
a [DsrC]-S-sulfo-L-cysteine = sulfite + a [DsrC protein]-disulfide
(2b)
-
-
-
hydrogen sulfide + a [DsrC protein]-disulfide = a [DsrC protein]-S-sulfanyl-L-cysteine
(1a)
-
-
-
a [DsrC protein]-trisulfide + NAD+ + 3 H2O = a [DsrC protein]-dithiol + sulfite + NADH + H+
sulfite is bound at an oxidation state of S1IV and immediately dehydrated. All oxygen atoms are fixed in a tight hydrogen-bonding network, upon transfer of two electrons to yield an S1II state, a second oxygen atom is released as water, but held within the active-site cavity. A further two-electron reduction leads to the S0 state, weakening the remaining S-O bond. With the final transfer of two electrons, the state of sulfide (S2II) is reached and a third water is released, catalytic mechanism overview. The heterobimetallic active-site heme 2 has a Cu(I) ion juxtaposed to a heme c at a Fe-Cu distance of 4.4 A. While the combination of metals is reminiscent of respiratory heme-copper oxidases, the oxidation-labile Cu(I) centre of MccA does not seem to undergo a redox transition during catalysis. Intact MccA tightly binds SO2 at heme 2, a dehydration product of the substrate sulfite that is partially turned over due to photoreduction by X-ray irradiation, yielding the reaction intermediate SO. Structure of sulfite reduction at heme2 of MccA, sulfite binds to the resting state of the enzyme, but the active-site architecture shifts the reversible dehydration equilibrium to SO2 + H2O. Reduction by two electrons occurs through photoreduction in the X-ray beam and leads to release of a second H2O after protonation, with SO remaining bound to the active site. A tight network of hydrogen bonds surrounds the bimetal centre and the bound substrate, holding the reaction products in place. The sulfite substrate only oxidizes half the heme groups of reduced MccA, emphasizing that the total electron charge of the multiheme enzyme is of high relevance for catalysis
a [DsrC protein]-trisulfide + NAD+ + 3 H2O = a [DsrC protein]-dithiol + sulfite + NADH + H+
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
[DsrC protein]-trisulfide,NAD+ oxidoreductase (sulfite-forming)
Contains siroheme. The enzyme is essential in prokaryotic sulfur-based energy metabolism, including sulfate/sulfite reducing organisms, sulfur-oxidizing bacteria, and organosulfonate reducers. The system comprises the DsrAB reductase and the DsrL protein, which form a tight complex. The reaction involves the small protein DsrC, which is present in all the organisms that contain dissimilatory sulfite reductase. In sulfite reducers the DsrL component transfers two electrons from NADH to the DsrAB component, which then reduces the sulfur in sulfite to an S(II) intermediate that forms (together with two cysteine residues of DsrC) a trisulfide. In sulfur oxidizers the enzyme catalyses the opposite reaction [1].
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
a [DsrC protein]-dithiol + sulfite + methyl viologen + H+
a [DsrC protein]-trisulfide + oxidized methyl viologen + 3 H2O
-
Substrates: -
Products: -
Products: -
?
a [DsrC protein]-dithiol + sulfite + NADH + H+
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
a [DsrC protein]-dithiol + sulfite + NADPH + H+
a [DsrC protein]-trisulfide + NADP+ + 3 H2O
-
Substrates: 20% activity compared to NADH as electron donor
Products: -
Products: -
?
hydrogen sulfide + a [DsrC protein]-disulfide + acceptor + H2O
sulfite + a [DsrC protein]-dithiol + reduced acceptor + H+
hydroxylamine + a [DsrC protein]-dithiol + 2 reduced acceptor + 2 H+
? + a [DsrC protein]-disulfide + 2 acceptor + 3 H2O
nitrite + a [DsrC protein]-dithiol + 2 reduced acceptor
? + a [DsrC protein]-disulfide + 2 acceptor + 2 H2O
nitrite + hydroxylamine
ammonia + ?
Substrates: -
Products: -
Products: -
?
sulfite + 6 ferrocytochrome c + 6 H+
sulfide + 6 ferricytochrome c + 3 H2O
Substrates: overall transfer of 6 electrons during the reaction
Products: -
Products: -
?
sulfite + a [DsrC protein]-dithiol + 2 reduced ferredoxin + 2 H+
hydrogen sulfide + a [DsrC protein]-disulfide + 2 oxidized ferredoxin + 3 H2O
sulfite + a [DsrC protein]-dithiol + reduced methyl viologen
trithionate + a [DsrC protein]-disulfide + oxidized methyl viologen
thiosulfate + reduced methyl viologen + H+
sulfide + oxidized methyl viologen
Substrates: highest activity
Products: -
Products: -
?
trithionate + reduced methyl viologen + H+
thiosulfate + sulfide + oxidized methyl viologen
Substrates: -
Products: -
Products: -
?
[DsrC protein]-dithiol + sulfite + NADH + H+
[DsrC protein]-trisulfide + NAD+ + 3 H2O
Substrates: the enzyme requires the action of its partner protein DsrC to catalyze a four-electron reduction of sulfite to a S0 valence state, in the form of a trisulfide bound to DsrC. The DsrC-trisulfide is believed to be later reduced to HS- and DsrC by the DsrMKJOP transmembrane complex
Products: -
Products: -
?
[DsrC protein]-dithiol + sulfite + reduced methyl viologen + H+
[DsrC protein]-trisulfide + oxidized methyl viologen + H2O
a [DsrC protein]-dithiol + sulfite + NADH + H+
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
-
Substrates: -
Products: -
Products: -
?
a [DsrC protein]-dithiol + sulfite + NADH + H+
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
-
Substrates: -
Products: -
Products: -
?
a [DsrC protein]-dithiol + sulfite + NADH + H+
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
-
Substrates: -
Products: -
Products: -
?
a [DsrC protein]-dithiol + sulfite + NADH + H+
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
Allochromatium vinosum U84760
-
Substrates: -
Products: -
Products: -
?
a [DsrC protein]-dithiol + sulfite + NADH + H+
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
-
Substrates: -
Products: -
Products: -
?
a [DsrC protein]-dithiol + sulfite + NADH + H+
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
-
Substrates: -
Products: -
Products: -
?
a [DsrC protein]-dithiol + sulfite + NADH + H+
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
-
Substrates: -
Products: -
Products: -
?
a [DsrC protein]-dithiol + sulfite + NADH + H+
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
-
Substrates: -
Products: -
Products: -
?
a [DsrC protein]-dithiol + sulfite + NADH + H+
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
-
Substrates: -
Products: -
Products: -
?
a [DsrC protein]-dithiol + sulfite + NADH + H+
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
-
Substrates: -
Products: -
Products: -
?
a [DsrC protein]-dithiol + sulfite + NADH + H+
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
-
Substrates: -
Products: -
Products: -
?
a [DsrC protein]-dithiol + sulfite + NADH + H+
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
-
Substrates: -
Products: -
Products: -
?
a [DsrC protein]-dithiol + sulfite + NADH + H+
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
-
Substrates: -
Products: -
Products: -
?
a [DsrC protein]-dithiol + sulfite + NADH + H+
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
-
Substrates: -
Products: -
Products: -
?
a [DsrC protein]-dithiol + sulfite + NADH + H+
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
-
Substrates: -
Products: -
Products: -
?
a [DsrC protein]-dithiol + sulfite + NADH + H+
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
-
Substrates: -
Products: -
Products: -
?
a [DsrC protein]-dithiol + sulfite + NADH + H+
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
-
Substrates: -
Products: -
Products: -
?
a [DsrC protein]-dithiol + sulfite + NADH + H+
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
-
Substrates: -
Products: -
Products: -
?
a [DsrC protein]-dithiol + sulfite + NADH + H+
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
-
Substrates: -
Products: -
Products: -
?
a [DsrC protein]-dithiol + sulfite + NADH + H+
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
-
Substrates: -
Products: -
Products: -
?
a [DsrC protein]-dithiol + sulfite + NADH + H+
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
-
Substrates: -
Products: -
Products: -
?
a [DsrC protein]-dithiol + sulfite + NADH + H+
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
-
Substrates: -
Products: -
Products: -
?
a [DsrC protein]-dithiol + sulfite + NADH + H+
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
-
Substrates: -
Products: -
Products: -
?
a [DsrC protein]-dithiol + sulfite + NADH + H+
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
-
Substrates: -
Products: -
Products: -
?
a [DsrC protein]-dithiol + sulfite + NADH + H+
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
Megalodesulfovibrio gigas No. 9332
-
Substrates: -
Products: -
Products: -
?
a [DsrC protein]-dithiol + sulfite + NADH + H+
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
-
Substrates: -
Products: -
Products: -
?
a [DsrC protein]-dithiol + sulfite + NADH + H+
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
-
Substrates: -
Products: -
Products: -
?
a [DsrC protein]-dithiol + sulfite + NADH + H+
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
-
Substrates: -
Products: -
Products: -
?
a [DsrC protein]-dithiol + sulfite + NADH + H+
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
-
Substrates: -
Products: -
Products: -
?
a [DsrC protein]-dithiol + sulfite + NADH + H+
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
-
Substrates: -
Products: -
Products: -
?
a [DsrC protein]-dithiol + sulfite + NADH + H+
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
-
Substrates: -
Products: -
Products: -
?
a [DsrC protein]-dithiol + sulfite + NADH + H+
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
-
Substrates: -
Products: -
Products: -
?
a [DsrC protein]-dithiol + sulfite + NADH + H+
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
-
Substrates: -
Products: -
Products: -
?
a [DsrC protein]-dithiol + sulfite + NADH + H+
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
-
Substrates: -
Products: -
Products: -
?
a [DsrC protein]-dithiol + sulfite + NADH + H+
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
-
Substrates: -
Products: -
Products: -
?
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
a [DsrC protein]-dithiol + sulfite + NADH + H+
Substrates: -
Products: -
Products: -
?
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
a [DsrC protein]-dithiol + sulfite + NADH + H+
Substrates: -
Products: -
Products: -
?
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
a [DsrC protein]-dithiol + sulfite + NADH + H+
Nitratidesulfovibrio vulgaris DSM 644
Substrates: -
Products: -
Products: -
?
hydrogen sulfide + a [DsrC protein]-disulfide + acceptor + H2O
sulfite + a [DsrC protein]-dithiol + reduced acceptor + H+
-
Substrates: -
Products: -
Products: -
?
hydrogen sulfide + a [DsrC protein]-disulfide + acceptor + H2O
sulfite + a [DsrC protein]-dithiol + reduced acceptor + H+
-
Substrates: -
Products: -
Products: -
?
hydrogen sulfide + a [DsrC protein]-disulfide + acceptor + H2O
sulfite + a [DsrC protein]-dithiol + reduced acceptor + H+
-
Substrates: -
Products: -
Products: -
?
hydrogen sulfide + a [DsrC protein]-disulfide + acceptor + H2O
sulfite + a [DsrC protein]-dithiol + reduced acceptor + H+
-
Substrates: -
Products: -
Products: -
?
hydrogen sulfide + a [DsrC protein]-disulfide + acceptor + H2O
sulfite + a [DsrC protein]-dithiol + reduced acceptor + H+
-
Substrates: -
Products: -
Products: -
?
hydrogen sulfide + a [DsrC protein]-disulfide + acceptor + H2O
sulfite + a [DsrC protein]-dithiol + reduced acceptor + H+
-
Substrates: -
Products: -
Products: -
?
hydrogen sulfide + a [DsrC protein]-disulfide + acceptor + H2O
sulfite + a [DsrC protein]-dithiol + reduced acceptor + H+
-
Substrates: -
Products: -
Products: -
?
hydrogen sulfide + a [DsrC protein]-disulfide + acceptor + H2O
sulfite + a [DsrC protein]-dithiol + reduced acceptor + H+
-
Substrates: -
Products: -
Products: -
?
hydrogen sulfide + a [DsrC protein]-disulfide + acceptor + H2O
sulfite + a [DsrC protein]-dithiol + reduced acceptor + H+
-
Substrates: -
Products: -
Products: -
?
hydrogen sulfide + a [DsrC protein]-disulfide + acceptor + H2O
sulfite + a [DsrC protein]-dithiol + reduced acceptor + H+
Nitratidesulfovibrio vulgaris Hildenborough
-
Substrates: -
Products: -
Products: -
?
hydrogen sulfide + a [DsrC protein]-disulfide + acceptor + H2O
sulfite + a [DsrC protein]-dithiol + reduced acceptor + H+
-
Substrates: -
Products: -
Products: -
?
hydrogen sulfide + a [DsrC protein]-disulfide + acceptor + H2O
sulfite + a [DsrC protein]-dithiol + reduced acceptor + H+
-
Substrates: -
Products: -
Products: -
?
hydrogen sulfite + H2O + ferrocytochrome c3
hydrogen sulfide + ferricytochrome c3
-
Substrates: -
Products: -
Products: -
?
hydrogen sulfite + H2O + ferrocytochrome c3
hydrogen sulfide + ferricytochrome c3
-
Substrates: -
Products: -
Products: -
?
hydroxylamine + a [DsrC protein]-dithiol + 2 reduced acceptor + 2 H+
? + a [DsrC protein]-disulfide + 2 acceptor + 3 H2O
-
Substrates: -
Products: -
Products: -
?
hydroxylamine + a [DsrC protein]-dithiol + 2 reduced acceptor + 2 H+
? + a [DsrC protein]-disulfide + 2 acceptor + 3 H2O
Nitratidesulfovibrio vulgaris Hildenborough
-
Substrates: -
Products: -
Products: -
?
hydroxylamine + methyl viologen + H+
ammonia + oxidized methyl viologen + H2O
-
Substrates: -
Products: -
Products: -
?
hydroxylamine + methyl viologen + H+
ammonia + oxidized methyl viologen + H2O
Nitratidesulfovibrio vulgaris NCIB 8303
-
Substrates: -
Products: -
Products: -
?
nitric oxide + methyl viologen + H+
?
-
Substrates: -
Products: -
Products: -
?
nitric oxide + methyl viologen + H+
?
Nitratidesulfovibrio vulgaris NCIB 8303
-
Substrates: -
Products: -
Products: -
?
nitrite + a [DsrC protein]-dithiol + 2 reduced acceptor
? + a [DsrC protein]-disulfide + 2 acceptor + 2 H2O
-
Substrates: -
Products: -
Products: -
?
nitrite + a [DsrC protein]-dithiol + 2 reduced acceptor
? + a [DsrC protein]-disulfide + 2 acceptor + 2 H2O
Nitratidesulfovibrio vulgaris Hildenborough
-
Substrates: -
Products: -
Products: -
?
nitrite + methyl viologen + H+
nitrate + oxidized methyl viologen + H2O
-
Substrates: -
Products: -
Products: -
?
nitrite + methyl viologen + H+
nitrate + oxidized methyl viologen + H2O
Nitratidesulfovibrio vulgaris NCIB 8303
-
Substrates: -
Products: -
Products: -
?
sulfite + a [DsrC protein]-dithiol + 2 reduced ferredoxin + 2 H+
hydrogen sulfide + a [DsrC protein]-disulfide + 2 oxidized ferredoxin + 3 H2O
-
Substrates: -
Products: overall reaction
Products: overall reaction
?
sulfite + a [DsrC protein]-dithiol + 2 reduced ferredoxin + 2 H+
hydrogen sulfide + a [DsrC protein]-disulfide + 2 oxidized ferredoxin + 3 H2O
Nitratidesulfovibrio vulgaris Hildenborough
-
Substrates: -
Products: overall reaction
Products: overall reaction
?
sulfite + a [DsrC protein]-dithiol + reduced methyl viologen
trithionate + a [DsrC protein]-disulfide + oxidized methyl viologen
-
Substrates: -
Products: trithionate is the major product, plus formation of thiosulfate and sulfid
Products: trithionate is the major product, plus formation of thiosulfate and sulfid
?
sulfite + a [DsrC protein]-dithiol + reduced methyl viologen
trithionate + a [DsrC protein]-disulfide + oxidized methyl viologen
-
Substrates: -
Products: trithionate is the major product, plus formation of thiosulfate and sulfid
Products: trithionate is the major product, plus formation of thiosulfate and sulfid
?
sulfite + a [DsrC protein]-dithiol + reduced methyl viologen
trithionate + a [DsrC protein]-disulfide + oxidized methyl viologen
-
Substrates: -
Products: trithionate is the major product with reduced methyl viologen as electron donor
Products: trithionate is the major product with reduced methyl viologen as electron donor
?
sulfite + methyl viologen + H+
sulfide + oxidized methyl viologen + H2O
-
Substrates: -
Products: -
Products: -
?
sulfite + methyl viologen + H+
sulfide + oxidized methyl viologen + H2O
Nitratidesulfovibrio vulgaris NCIB 8303
-
Substrates: -
Products: -
Products: -
?
sulfite + reduced acceptor + H+
hydrogen sulfide + oxidized acceptor
-
Substrates: -
Products: -
Products: -
?
sulfite + reduced acceptor + H+
hydrogen sulfide + oxidized acceptor
-
Substrates: -
Products: -
Products: -
?
sulfite + reduced methyl viologen + H+
hydrogen sulfide + oxidized methyl viologen
Substrates: -
Products: -
Products: -
?
sulfite + reduced methyl viologen + H+
hydrogen sulfide + oxidized methyl viologen
-
Substrates: -
Products: -
Products: -
?
sulfite + reduced methyl viologen + H+
hydrogen sulfide + oxidized methyl viologen
-
Substrates: -
Products: -
Products: -
?
sulfite + reduced methyl viologen + H+
hydrogen sulfide + oxidized methyl viologen
-
Substrates: -
Products: -
Products: -
?
sulfite + reduced methyl viologen + H+
hydrogen sulfide + oxidized methyl viologen
-
Substrates: -
Products: -
Products: -
?
[DsrC protein]-dithiol + sulfite + reduced methyl viologen + H+
[DsrC protein]-trisulfide + oxidized methyl viologen + H2O
Substrates: DsrC is a cosubstrate for sulfite reduction by the enzyme
Products: -
Products: -
?
[DsrC protein]-dithiol + sulfite + reduced methyl viologen + H+
[DsrC protein]-trisulfide + oxidized methyl viologen + H2O
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: the DsrABL complex effectively catalyzes NADH-dependent sulfite reduction, which is strongly enhanced by the sulphur-binding protein DsrC. DsrL exhibits NAD(P)H:acceptor oxidoreductase activity with a strong preference for NADH over NADPH
Products: -
Products: -
-
additional information
?
-
-
Substrates: DsrC is essential for the function of DsrAB. DsrC transfers the sulfur to the enzyme acting in the oxidative direction, i.e. in reverse of the reaction catalyzed in sulfate reducers
Products: -
Products: -
-
additional information
?
-
-
Substrates: DsrC is essential for the function of DsrAB. DsrC transfers the sulfur to the enzyme acting in the oxidative direction, i.e. in reverse of the reaction catalyzed in sulfate reducers
Products: -
Products: -
-
additional information
?
-
-
Substrates: DsrC is essential for the function of DsrAB. DsrC transfers the sulfur to the enzyme acting in the oxidative direction, i.e. in reverse of the reaction catalyzed in sulfate reducers
Products: -
Products: -
-
additional information
?
-
Substrates: the enzyme catalyzes the reduction of sulfite to sulfide
Products: -
Products: -
?
additional information
?
-
Cryptococcus deneoformans ATCC MYA-565
Substrates: the enzyme catalyzes the reduction of sulfite to sulfide
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme catalyzes the reduction of sulfite to sulfide
Products: -
Products: -
?
additional information
?
-
-
Substrates: DsrC is essential for the function of DsrAB. DsrC transfers the sulfur to the enzyme acting in the oxidative direction, i.e. in reverse of the reaction catalyzed in sulfate reducers
Products: -
Products: -
-
additional information
?
-
-
Substrates: DsrC is essential for the function of DsrAB. DsrC transfers the sulfur to the enzyme acting in the oxidative direction, i.e. in reverse of the reaction catalyzed in sulfate reducers
Products: -
Products: -
-
additional information
?
-
-
Substrates: DsrC is essential for the function of DsrAB. DsrC transfers the sulfur to the enzyme acting in the oxidative direction, i.e. in reverse of the reaction catalyzed in sulfate reducers
Products: -
Products: -
-
additional information
?
-
-
Substrates: DsrC is essential for the function of DsrAB. DsrC transfers the sulfur to the enzyme acting in the oxidative direction, i.e. in reverse of the reaction catalyzed in sulfate reducers
Products: -
Products: -
-
additional information
?
-
-
Substrates: DsrC is essential for the function of DsrAB. DsrC transfers the sulfur to the enzyme acting in the oxidative direction, i.e. in reverse of the reaction catalyzed in sulfate reducers
Products: -
Products: -
-
additional information
?
-
-
Substrates: DsrC is essential for the function of DsrAB. DsrC transfers the sulfur to the enzyme acting in the oxidative direction, i.e. in reverse of the reaction catalyzed in sulfate reducers
Products: -
Products: -
-
additional information
?
-
-
Substrates: DsrC is essential for the function of DsrAB. DsrC transfers the sulfur to the enzyme acting in the oxidative direction, i.e. in reverse of the reaction catalyzed in sulfate reducers
Products: -
Products: -
-
additional information
?
-
-
Substrates: DsrC is essential for the function of DsrAB. DsrC transfers the sulfur to the enzyme acting in the oxidative direction, i.e. in reverse of the reaction catalyzed in sulfate reducers
Products: -
Products: -
-
additional information
?
-
-
Substrates: DsrC is essential for the function of DsrAB. DsrC transfers the sulfur to the enzyme acting in the oxidative direction, i.e. in reverse of the reaction catalyzed in sulfate reducers
Products: -
Products: -
-
additional information
?
-
-
Substrates: the enzyme reduces sulfite mainly to trithionate besides thiosulfate and sulfide in vitro
Products: -
Products: -
-
additional information
?
-
-
Substrates: DsrC is essential for the function of DsrAB. DsrC transfers the sulfur to the enzyme acting in the oxidative direction, i.e. in reverse of the reaction catalyzed in sulfate reducers
Products: -
Products: -
-
additional information
?
-
-
Substrates: two-state hypothesis for enzyme activity: an active form (DVa) binds and catalyzes substrate reduction, and an inactive form (DVi) exists for the resting enzyme. Only the active form of the enzyme need be considered during steady-state turnover. Determination of the rate constants defining these structural perturbations, from oxidized to reduced and reduced to oxidized states
Products: -
Products: -
?
additional information
?
-
Substrates: DsrC works as co-substrate of the enzyme. The enzyme contains a coupled siroheme-[4Fe-4S] cofactor that binds sulfite, which is reduced to a DsrC trisulfide where sulfite-derived S0 is bound between two conserved DsrC cysteine residues. The DsrC trisulfide is a key intermediate in sulfate/sulfite reduction and is proposed to be reduced by the DsrMKJOP transmembrane complex with production of sulfide and reduced DsrC, in a process that is likely coupled with energy conservation
Products: -
Products: -
-
additional information
?
-
-
Substrates: the enzyme does not form an alkaline ferrohemochromogen, is not reduced with dithionite or borohydride, and does not form a spectrally visible complex with CO. Thiosulfate, trithionate, and tetrathionate are not reduced by the enzyme. No activity with NADH or NADPH
Products: -
Products: -
-
additional information
?
-
Substrates: DsrC is essential for the function of DsrAB. DsrC transfers the sulfur to the enzyme acting in the oxidative direction, i.e. in reverse of the reaction catalyzed in sulfate reducers
Products: -
Products: -
-
additional information
?
-
Nitratidesulfovibrio vulgaris Hildenborough
-
Substrates: two-state hypothesis for enzyme activity: an active form (DVa) binds and catalyzes substrate reduction, and an inactive form (DVi) exists for the resting enzyme. Only the active form of the enzyme need be considered during steady-state turnover. Determination of the rate constants defining these structural perturbations, from oxidized to reduced and reduced to oxidized states
Products: -
Products: -
?
additional information
?
-
Nitratidesulfovibrio vulgaris NCIB 8303
-
Substrates: the enzyme does not form an alkaline ferrohemochromogen, is not reduced with dithionite or borohydride, and does not form a spectrally visible complex with CO. Thiosulfate, trithionate, and tetrathionate are not reduced by the enzyme. No activity with NADH or NADPH
Products: -
Products: -
-
additional information
?
-
-
Substrates: DsrC is essential for the function of DsrAB. DsrC transfers the sulfur to the enzyme acting in the oxidative direction, i.e. in reverse of the reaction catalyzed in sulfate reducers
Products: -
Products: -
-
additional information
?
-
-
Substrates: DsrC is essential for the function of DsrAB. DsrC transfers the sulfur to the enzyme acting in the oxidative direction, i.e. in reverse of the reaction catalyzed in sulfate reducers
Products: -
Products: -
-
additional information
?
-
-
Substrates: DsrC is essential for the function of DsrAB. DsrC transfers the sulfur to the enzyme acting in the oxidative direction, i.e. in reverse of the reaction catalyzed in sulfate reducers
Products: -
Products: -
-
additional information
?
-
-
Substrates: DsrC is essential for the function of DsrAB. DsrC transfers the sulfur to the enzyme acting in the oxidative direction, i.e. in reverse of the reaction catalyzed in sulfate reducers
Products: -
Products: -
-
additional information
?
-
-
Substrates: DsrC is essential for the function of DsrAB. DsrC transfers the sulfur to the enzyme acting in the oxidative direction, i.e. in reverse of the reaction catalyzed in sulfate reducers
Products: -
Products: -
-
additional information
?
-
Substrates: multiheme cytochrome c enzymes catalyse complex-multi-electron redox reactions and bind their substrates through the free electron pairs of a heteroatom to a free coordination position at an active-site hem group. Electrons are then provided or accepted by the tightly coupled chain of heme groups
Products: -
Products: -
?
additional information
?
-
Substrates: MccA reduces sulfite, but not arsenate, selenate, selenite, hydroxylamine, hydrazine, fumarate, nitrate, thiosulfate, tetrathionate, polysulfide, or Fe(III). Nitrite is reduced only very slowly to ammonium
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
a [DsrC protein]-dithiol + sulfite + NADH + H+
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
hydrogen sulfide + a [DsrC protein]-disulfide + acceptor + H2O
sulfite + a [DsrC protein]-dithiol + reduced acceptor + H+
sulfite + 6 ferrocytochrome c + 6 H+
sulfide + 6 ferricytochrome c + 3 H2O
Substrates: overall transfer of 6 electrons during the reaction
Products: -
Products: -
?
[DsrC protein]-dithiol + sulfite + NADH + H+
[DsrC protein]-trisulfide + NAD+ + 3 H2O
Substrates: the enzyme requires the action of its partner protein DsrC to catalyze a four-electron reduction of sulfite to a S0 valence state, in the form of a trisulfide bound to DsrC. The DsrC-trisulfide is believed to be later reduced to HS- and DsrC by the DsrMKJOP transmembrane complex
Products: -
Products: -
?
[DsrC protein]-dithiol + sulfite + reduced methyl viologen + H+
[DsrC protein]-trisulfide + oxidized methyl viologen + H2O
Substrates: DsrC is a cosubstrate for sulfite reduction by the enzyme
Products: -
Products: -
?
additional information
?
-
Substrates: multiheme cytochrome c enzymes catalyse complex-multi-electron redox reactions and bind their substrates through the free electron pairs of a heteroatom to a free coordination position at an active-site hem group. Electrons are then provided or accepted by the tightly coupled chain of heme groups
Products: -
Products: -
?
a [DsrC protein]-dithiol + sulfite + NADH + H+
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
-
Substrates: -
Products: -
Products: -
?
a [DsrC protein]-dithiol + sulfite + NADH + H+
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
-
Substrates: -
Products: -
Products: -
?
a [DsrC protein]-dithiol + sulfite + NADH + H+
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
-
Substrates: -
Products: -
Products: -
?
a [DsrC protein]-dithiol + sulfite + NADH + H+
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
Allochromatium vinosum U84760
-
Substrates: -
Products: -
Products: -
?
a [DsrC protein]-dithiol + sulfite + NADH + H+
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
-
Substrates: -
Products: -
Products: -
?
a [DsrC protein]-dithiol + sulfite + NADH + H+
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
-
Substrates: -
Products: -
Products: -
?
a [DsrC protein]-dithiol + sulfite + NADH + H+
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
-
Substrates: -
Products: -
Products: -
?
a [DsrC protein]-dithiol + sulfite + NADH + H+
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
-
Substrates: -
Products: -
Products: -
?
a [DsrC protein]-dithiol + sulfite + NADH + H+
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
-
Substrates: -
Products: -
Products: -
?
a [DsrC protein]-dithiol + sulfite + NADH + H+
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
-
Substrates: -
Products: -
Products: -
?
a [DsrC protein]-dithiol + sulfite + NADH + H+
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
-
Substrates: -
Products: -
Products: -
?
a [DsrC protein]-dithiol + sulfite + NADH + H+
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
-
Substrates: -
Products: -
Products: -
?
a [DsrC protein]-dithiol + sulfite + NADH + H+
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
-
Substrates: -
Products: -
Products: -
?
a [DsrC protein]-dithiol + sulfite + NADH + H+
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
-
Substrates: -
Products: -
Products: -
?
a [DsrC protein]-dithiol + sulfite + NADH + H+
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
-
Substrates: -
Products: -
Products: -
?
a [DsrC protein]-dithiol + sulfite + NADH + H+
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
-
Substrates: -
Products: -
Products: -
?
a [DsrC protein]-dithiol + sulfite + NADH + H+
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
-
Substrates: -
Products: -
Products: -
?
a [DsrC protein]-dithiol + sulfite + NADH + H+
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
-
Substrates: -
Products: -
Products: -
?
a [DsrC protein]-dithiol + sulfite + NADH + H+
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
-
Substrates: -
Products: -
Products: -
?
a [DsrC protein]-dithiol + sulfite + NADH + H+
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
-
Substrates: -
Products: -
Products: -
?
a [DsrC protein]-dithiol + sulfite + NADH + H+
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
-
Substrates: -
Products: -
Products: -
?
a [DsrC protein]-dithiol + sulfite + NADH + H+
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
-
Substrates: -
Products: -
Products: -
?
a [DsrC protein]-dithiol + sulfite + NADH + H+
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
-
Substrates: -
Products: -
Products: -
?
a [DsrC protein]-dithiol + sulfite + NADH + H+
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
-
Substrates: -
Products: -
Products: -
?
a [DsrC protein]-dithiol + sulfite + NADH + H+
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
Megalodesulfovibrio gigas No. 9332
-
Substrates: -
Products: -
Products: -
?
a [DsrC protein]-dithiol + sulfite + NADH + H+
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
-
Substrates: -
Products: -
Products: -
?
a [DsrC protein]-dithiol + sulfite + NADH + H+
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
-
Substrates: -
Products: -
Products: -
?
a [DsrC protein]-dithiol + sulfite + NADH + H+
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
-
Substrates: -
Products: -
Products: -
?
a [DsrC protein]-dithiol + sulfite + NADH + H+
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
-
Substrates: -
Products: -
Products: -
?
a [DsrC protein]-dithiol + sulfite + NADH + H+
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
-
Substrates: -
Products: -
Products: -
?
a [DsrC protein]-dithiol + sulfite + NADH + H+
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
-
Substrates: -
Products: -
Products: -
?
a [DsrC protein]-dithiol + sulfite + NADH + H+
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
-
Substrates: -
Products: -
Products: -
?
a [DsrC protein]-dithiol + sulfite + NADH + H+
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
-
Substrates: -
Products: -
Products: -
?
a [DsrC protein]-dithiol + sulfite + NADH + H+
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
-
Substrates: -
Products: -
Products: -
?
a [DsrC protein]-dithiol + sulfite + NADH + H+
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
-
Substrates: -
Products: -
Products: -
?
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
a [DsrC protein]-dithiol + sulfite + NADH + H+
Substrates: -
Products: -
Products: -
?
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
a [DsrC protein]-dithiol + sulfite + NADH + H+
Substrates: -
Products: -
Products: -
?
a [DsrC protein]-trisulfide + NAD+ + 3 H2O
a [DsrC protein]-dithiol + sulfite + NADH + H+
Nitratidesulfovibrio vulgaris DSM 644
Substrates: -
Products: -
Products: -
?
hydrogen sulfide + a [DsrC protein]-disulfide + acceptor + H2O
sulfite + a [DsrC protein]-dithiol + reduced acceptor + H+
-
Substrates: -
Products: -
Products: -
?
hydrogen sulfide + a [DsrC protein]-disulfide + acceptor + H2O
sulfite + a [DsrC protein]-dithiol + reduced acceptor + H+
-
Substrates: -
Products: -
Products: -
?
hydrogen sulfide + a [DsrC protein]-disulfide + acceptor + H2O
sulfite + a [DsrC protein]-dithiol + reduced acceptor + H+
-
Substrates: -
Products: -
Products: -
?
hydrogen sulfide + a [DsrC protein]-disulfide + acceptor + H2O
sulfite + a [DsrC protein]-dithiol + reduced acceptor + H+
-
Substrates: -
Products: -
Products: -
?
hydrogen sulfide + a [DsrC protein]-disulfide + acceptor + H2O
sulfite + a [DsrC protein]-dithiol + reduced acceptor + H+
-
Substrates: -
Products: -
Products: -
?
hydrogen sulfide + a [DsrC protein]-disulfide + acceptor + H2O
sulfite + a [DsrC protein]-dithiol + reduced acceptor + H+
-
Substrates: -
Products: -
Products: -
?
hydrogen sulfide + a [DsrC protein]-disulfide + acceptor + H2O
sulfite + a [DsrC protein]-dithiol + reduced acceptor + H+
-
Substrates: -
Products: -
Products: -
?
hydrogen sulfide + a [DsrC protein]-disulfide + acceptor + H2O
sulfite + a [DsrC protein]-dithiol + reduced acceptor + H+
-
Substrates: -
Products: -
Products: -
?
hydrogen sulfide + a [DsrC protein]-disulfide + acceptor + H2O
sulfite + a [DsrC protein]-dithiol + reduced acceptor + H+
-
Substrates: -
Products: -
Products: -
?
hydrogen sulfide + a [DsrC protein]-disulfide + acceptor + H2O
sulfite + a [DsrC protein]-dithiol + reduced acceptor + H+
Nitratidesulfovibrio vulgaris Hildenborough
-
Substrates: -
Products: -
Products: -
?
hydrogen sulfide + a [DsrC protein]-disulfide + acceptor + H2O
sulfite + a [DsrC protein]-dithiol + reduced acceptor + H+
-
Substrates: -
Products: -
Products: -
?
hydrogen sulfide + a [DsrC protein]-disulfide + acceptor + H2O
sulfite + a [DsrC protein]-dithiol + reduced acceptor + H+
-
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
heme
octaheme cytochrome, a homotrimer with an unprecedented fold and heme arrangement, as well as a heme bound to a CX15CH motif. The heterobimetallic active-site heme 2 has a Cu(I) ion juxtaposed to a heme c at a Fe-Cu distance of 4.4 A, active-site heme 2 is bound to a canonical CXXCH motif with H306 as a proximal axial ligand. In the CX15CH motif of heme 8, the extended region between the two cysteine residues forms a loop with a short helical turn, in direct vicinity to another loop harbouring the only non-proline cis peptide in the enzyme, between residues G508 and F509. Its formation might require the essential peptidyl isomerase MccB2, and it is presumed to be a prerequisite for correct folding of the loop in the maturation process of heme 8, which is likely to be attached by the dedicated cytochrome c synthase CcsA1. The structure of the CX15CH heme c binding motif disrupts the general parallel/perpendicular heme stacking sequence, and rotates the heme out of plane, possibly to optimize the interaction with the putative electron donor, the iron-sulfur protein MccC
siroheme
O93650; O93651
binding of two sirohemes and four [4Fe-4S]-clusters per alpha2beta2 structure
siroheme
Q9ZH18; Q9ZH17
binding of two sirohemes and four [4Fe-4S]-clusters per alpha2beta2 structure
siroheme
protein complex contains two siroheme-[4Fe4S] cofactors bound by subunit DsrB, two sirohydrochlorins and two [4Fe-4S]-centers bound by subunit DsrA, and another four [4Fe-4S]-centers in the ferredoxin domains
siroheme
-
at least two of three subunits contain two pairs of [Fe4-S4]-centers and siroheme units
siroheme
-
close to 80% of the siroheme moiety in the enzyme is demetallated
tetrahydroporphyrin
-
contains 2 tetrahydroporphyrin groups per molecule
-
tetrahydroporphyrin
-
contains 2 tetrahydroporphyrin groups per molecule, about 80% of the tetrahydroporphyrin groups do not contain iron
-
[4Fe-4S]-center
O93650; O93651
binding of two sirohemes and four [4Fe-4S]-clusters per alpha2beta2 structure
[4Fe-4S]-center
Q9ZH18; Q9ZH17
binding of two sirohemes and four [4Fe-4S]-clusters per alpha2beta2 structure
[4Fe-4S]-center
protein complex contains two siroheme-[4Fe4S] cofactors bound by subunit DsrB, two sirohydrochlorins and two [4Fe-4S]-centers bound by subunit DsrA, and another four [4Fe-4S]-centers in the ferredoxin domains
[4Fe-4S]-center
-
at least two of three subunits contain two pairs of [Fe4-S4]-centers and siroheme units
[4Fe-4S]-center
the enzyme contains 8 [4Fe-4S]-centers
additional information
DsrD as allosteric activator of the enzyme's sulfite reduction activity. In the presence of DsrD, the maximum activity of sulfite reduction by the enzyme doubles relative to its absence
-
additional information
-
the enzyme does not contain significant amounts of FAD or FMN
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Cu
the heterobimetallic active-site heme 2 has a Cu(I) ion juxtaposed to a heme c at a Fe-Cu distance of 4.4 A. While the combination of metals is reminiscent of respiratory hemecopper oxidases, the oxidation-labile Cu(I) centre of MccA does not seem to undergo a redox transition during catalysis. The copper-depleted form II of MccA, the absence of the heterometal allows for a binding mode of sulfite that is similar to the one seen in the siroheme-containing enzymes or in NrfA. In the structure of the Cu-containing, high-activity form I of MccA, all 12 monomers in the asymmetric unit have a ligand bound to heme 2
Fe
the heterobimetallic active-site heme 2 has a Cu(I) ion juxtaposed to a heme c at a Fe-Cu distance of 4.4 A
Iron
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.011
sulfite
in the absence of DsrC, at pH 7.0 and 60°C
0.012
sulfite
in the presence of DsrD, at pH 7.0 and 60°C
0.012
sulfite
in the presence of DsrC, at pH 7.0 and 60°C
0.013
sulfite
in the absence of DsrD, at pH 7.0 and 60°C
0.0135
sulfite
-
with methyl viologen as cosubstrate, at pH 7.0 and 30°C
3.1
sulfite
-
pH 6.0, temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 6
7.5
6
pH optimum with thiosulfate and sulfite as substrates
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
31
65
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
O93650 i.e. subunit DsrA, O93651 i.e. subunit DsrB
O93650; O93651
UniProt
brenda
O93650 i.e. subunit DsrA, O93651 i.e. subunit DsrB
O93650; O93651
UniProt
brenda
Q9ZH18 i.e. subunit DsrA, Q9ZH17 i.e. subunit DsrB
Q9ZH18; Q9ZH17
UniProt
brenda
Nitratidesulfovibrio vulgaris Hildenborough
O33909 i.e. subunit DsrA, O33910 i.e. subunit DsrB
O33909; O33910
UniProt
brenda
subunit A
UniProt
brenda
subunit A
UniProt
brenda
subunits a and b
Q2M446; Q2M447, Q2M449; Q2M448, Q2M451; Q2M450, Q2M453; Q2M452, Q2M455; Q2M454, Q2M456; Q2M457, Q2M459; Q2M458, Q2M460; Q2M461, Q2M463; Q2M462, Q2M464; Q2M465, Q2M466; Q2M467, Q2M468; Q2M469, Q2M471; Q2M470, Q2M472; Q2M473, Q2M475; Q2M474, Q2M476; Q2M477, Q2M479; Q2M478, Q2M481; Q2M480, Q2M483; Q2M482, Q2M485; Q2M484, Q2M487; Q2M486
UniProt
brenda
Q59109 i.e. subunit DsrA, Q59110 i.e. subunit DsrB
UniProt
brenda
P45574 i.e. subunit alpha, P45575 i.e. subunit beta
UniProt
brenda
subunits alpha and beta
UniProt
brenda
Nitratidesulfovibrio vulgaris Hildenborough
P45574 i.e. subunit alpha, P45575 i.e. subunit beta
UniProt
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
O33998; D3RSN2
the sulfur globules of Allochromatium vinosum are located in the extracytoplasmic space whilst the dissimilatory sulfite reductase appear to be either cytoplasmic or membrane-bound
brenda
-
the sulfur globules of Allochromatium vinosum are located in the extracytoplasmic space whilst the dissimilatory sulfite reductase appear to be either cytoplasmic or membrane-bound
-
brenda
O33998; D3RSN2
the sulfur globules of Allochromatium vinosum are located in the extracytoplasmic space whilst the dissimilatory sulfite reductase appear to be either cytoplasmic or membrane-bound
brenda
-
the sulfur globules of Allochromatium vinosum are located in the extracytoplasmic space whilst the dissimilatory sulfite reductase appear to be either cytoplasmic or membrane-bound
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
MccA belongs to the genetically diverse family of multiheme c enzymes and has eight heme groups covalently attached to conserved heme-binding motifs in the peptide sequence. Multiheme cytochrome c enzymes show a high conservation of heme group arrangements, but not of sequence, with recurring heme-packing motifs that result in either a parallel or a perpendicular packing of two of the moieties. They catalyse complexmulti-electron redox reactions and bind their substrates through the free electron pairs of a heteroatom to a free coordination position at an active-site hem group. Electrons are then provided or accepted by the tightly coupled chain of heme groups
metabolism
physiological function
additional information
anoxically purified MccA exhibits a 2 to 5.5fold higher specific sulfite reductase activity than the enzyme isolated under oxic conditions. Presence of two cysteine residues, C399 and C495, juxtaposed at the distal side of the active-site cavity. The active site is a shallow cavity on the distal side of heme 2, lined by residues K208, Y285, Y301, R366 and K393, which are conserved among MccA orthologues
metabolism
-
DsrC is a key protein in dissimilatory sulfite reduction
metabolism
the enzyme encoded by MET5 is involved in the sulfur metabolic pathway in the sulfur assimilation of Cryptococcus neoformans, overview. Sulfate is used by the active MET3, MET14, MET5, and MET10 genes in the sulfate assimilation pathway
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
metabolism
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
-
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
-
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
-
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
-
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
-
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
-
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
-
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
-
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
-
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
-
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
-
metabolism
Pelodictyon clathratiforme DSM 5477
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
-
metabolism
Cryptococcus deneoformans ATCC MYA-565
-
the enzyme encoded by MET5 is involved in the sulfur metabolic pathway in the sulfur assimilation of Cryptococcus neoformans, overview. Sulfate is used by the active MET3, MET14, MET5, and MET10 genes in the sulfate assimilation pathway
-
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
-
metabolism
Nitratidesulfovibrio vulgaris DSM 644
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
-
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
-
metabolism
-
the enzyme encoded by MET5 is involved in the sulfur metabolic pathway in the sulfur assimilation of Cryptococcus neoformans, overview. Sulfate is used by the active MET3, MET14, MET5, and MET10 genes in the sulfate assimilation pathway
-
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
-
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
-
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
-
metabolism
Thiocystis violacea DSM 208
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
-
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
-
metabolism
Thiocystis gelatinosa DSM 215
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
-
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
-
metabolism
Thiocapsa rosea DSM 235
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
-
metabolism
Thiocapsa marina DSM 5653
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
-
metabolism
Thiobaca trueperi DSM 13587
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
-
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
-
metabolism
Halochromatium salexigens DSM 4395
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
-
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
-
metabolism
Marichromatium gracile DSM 203
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
-
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
-
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
-
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
-
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
-
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
-
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
-
metabolism
Thioalkalivibrio thiocyanodenitrificans DSM 16954
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
-
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
-
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
-
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
-
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
-
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
-
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
-
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
-
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
-
metabolism
Prosthecochloris vibrioformis DSM 261
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
-
metabolism
Chlorobium phaeovibrioides DSM 269
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
-
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
-
metabolism
-
key microbial enzyme in both the reductive and the oxidative steps of the biogeochemical sulfur cycle
-
physiological function
O33998; D3RSN2
polar insertion mutations immediately upstream of dsrA, and in dsrB, in the gene cluster dsrABEFHCMK lead to an inability of the cells to oxidize intracellularly stored sulfur. The capability of the mutants to oxidize sulfide, thiosulfate and sulfite under photolithoautotrophic conditions is unaltered. Photoorganoheterotrophic growth is also unaffected
physiological function
sulfur globule oxidation is strictly dependent on the dissimilatory sulfite reductase system. Deletion of dsrM or dsrT, or the two dsrCABL clusters abolishes sulfur globule oxidation and prevents formation of sulfate from sulfide. The DSR system also seems to be involved in the formation of thiosulfate. The dsr mutants incapable of complete substrate oxidation oxidizes sulfide and thiosulfate about twice as fast as the wild-type, while having only slightly lower growth rates of 7080% of wild-type
physiological function
Soil bacterium
-
in salt marsh sediments exposed to acid mine drainage for over 100 years, recovered dsrAB sequences of dissimilatory sulfite redactase genes from three sites indicate the dominance of a single Desulfovibrio species. Other major sequence clades are related most closely to Desulfosarcina, Desulfococcus, Desulfobulbus, and Desulfosporosinus species. The presence of metal sulfides with low delta34S values relative to delta34S values of pore water sulfate show that sediment sulfate-reducing bacteria populations are actively reducing sulfate under ambient conditions (pH of about 2), although possibly within less acidic microenvironments. Findings imply a highly dynamic microbially mediated cycling of sulfate and sulfide, and thus the speciation and mobility of chalcophilic contaminant metal(loid)s in acid mine drainage-impacted marsh sediments
physiological function
-
the QmoABC membrane complex is essential for efficient electron delivery to AprAB, in order to sustain catalysis. Direct electron transfer occurs AprAB and the QmoABC complex, coupling the quinone-pool to sulfate reduction
physiological function
the Epsilonproteobacterium Wolinella succinogenes does not encode a siroheme sulfite reductase and the nrfA gene is not induced during sulfite respiration. Instead, sulfite is reduced by the octaheme c-type cytochrome MccA, with sulfide as the sole product. The enzyme MccA catalyzes the six-electron reduction of sulfite to sulfide, the pivot point of the biogeochemical cycle of the element sulfur for dissimilatory sulfite utilization. It is distinct from known sulfite reductases because it has a substantially higher catalytic activity and a relatively low reactivity towards nitrite
physiological function
the sulfite reductase MET5 gene confers Cys auxotrophy
physiological function
-
the enzyme reduces sulfite to a sulfide as the main source of energy in the anaerobic bacterium Desulphovibrio gigas
physiological function
Megalodesulfovibrio gigas No. 9332
-
the enzyme reduces sulfite to a sulfide as the main source of energy in the anaerobic bacterium Desulphovibrio gigas
-
physiological function
-
polar insertion mutations immediately upstream of dsrA, and in dsrB, in the gene cluster dsrABEFHCMK lead to an inability of the cells to oxidize intracellularly stored sulfur. The capability of the mutants to oxidize sulfide, thiosulfate and sulfite under photolithoautotrophic conditions is unaltered. Photoorganoheterotrophic growth is also unaffected
-
physiological function
-
sulfur globule oxidation is strictly dependent on the dissimilatory sulfite reductase system. Deletion of dsrM or dsrT, or the two dsrCABL clusters abolishes sulfur globule oxidation and prevents formation of sulfate from sulfide. The DSR system also seems to be involved in the formation of thiosulfate. The dsr mutants incapable of complete substrate oxidation oxidizes sulfide and thiosulfate about twice as fast as the wild-type, while having only slightly lower growth rates of 7080% of wild-type
-
physiological function
Cryptococcus deneoformans ATCC MYA-565
-
the sulfite reductase MET5 gene confers Cys auxotrophy
-
physiological function
-
the sulfite reductase MET5 gene confers Cys auxotrophy
-
physiological function
-
the enzyme reduces sulfite to a sulfide as the main source of energy in the anaerobic bacterium Desulphovibrio gigas
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). DSRA_ALLVD
Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D)
417
0
46791
Swiss-Prot
-
DSVC_NITV2
Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough)
105
0
11873
Swiss-Prot
-
DSVB_NITV2
Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough)
381
0
42519
Swiss-Prot
-
DSVB_MEGG1
Megalodesulfovibrio gigas (strain ATCC 19364 / DSM 1382 / NCIMB 9332 / VKM B-1759)
262
0
28569
Swiss-Prot
-
DSRB_ARCFU
Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)
366
0
41570
Swiss-Prot
-
DSRA_ARCFU
Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)
418
0
47525
Swiss-Prot
-
O28055_ARCFU
Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)
115
0
13478
TrEMBL
-
DSVA_NITV2
Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough)
437
0
49091
Swiss-Prot
-
Q5K8J1_CRYD1
Cryptococcus deneoformans (strain JEC21 / ATCC MYA-565)
1375
0
149363
TrEMBL
-
MCCA_WOLSU
Wolinella succinogenes (strain ATCC 29543 / DSM 1740 / CCUG 13145 / JCM 31913 / LMG 7466 / NCTC 11488 / FDC 602W)
702
0
78939
Swiss-Prot
Secretory Pathway (Reliability: 3)
Q8K5E9_CHLTE
Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS)
416
0
46351
TrEMBL
Secretory Pathway (Reliability: 4)
Q8ZUX1_PYRAE
Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2)
111
0
12669
TrEMBL
Secretory Pathway (Reliability: 2)
Q93TQ6_9DELT
305
0
33420
TrEMBL
Secretory Pathway (Reliability: 1)
Q93TQ7_9DELT
155
0
16778
TrEMBL
-
Q93TQ8_9DELT
157
0
17517
TrEMBL
Secretory Pathway (Reliability: 2)
Q93TQ9_9DELT
99
0
11183
TrEMBL
-
Q93TR0_9DELT
164
0
18359
TrEMBL
-
Q93TR1_9DELT
288
0
32663
TrEMBL
Secretory Pathway (Reliability: 3)
Q93TR2_9DELT
137
0
16015
TrEMBL
-
Q93TR3_9DELT
302
0
33813
TrEMBL
-
Q93TR4_9DELT
311
0
34495
TrEMBL
-
Q93TR5_9DELT
161
0
17929
TrEMBL
Chloroplast (Reliability: 4)
Q93TR6_9DELT
206
0
22572
TrEMBL
Mitochondrion (Reliability: 2)
Q93TR7_9DELT
324
0
35807
TrEMBL
other Location (Reliability: 2)
Q93TR8_9DELT
346
0
38536
TrEMBL
Mitochondrion (Reliability: 4)
Q93TR9_9DELT
326
0
36286
TrEMBL
-
Q93TS0_DESOH
Desulfosudis oleivorans (strain DSM 6200 / JCM 39069 / Hxd3)
312
0
34462
TrEMBL
-
Q93TS2_9DELT
310
0
34995
TrEMBL
-
Q93TS3_9DELT
182
0
20273
TrEMBL
Secretory Pathway (Reliability: 1)
Q93TS4_9DELT
186
0
20960
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
11000
-
2 * 50000, alpha-subunit, + 2 * 45000, beta subunit, + 1-3 * 11000, gamma-subunit. The gamma-subunit seems not to be an integral part of the protein
170000
200000
41200
O33909; O33910
2 * 44200, alpha-subunit, + 2 * 41200, beta-subunit
44200
O33909; O33910
2 * 44200, alpha-subunit, + 2 * 41200, beta-subunit
45000
-
2 * 50000, alpha-subunit, + 2 * 45000, beta subunit, + 1-3 * 11000, gamma-subunit. The gamma-subunit seems not to be an integral part of the protein
48000
-
2 * 48000, alpha-subunit, 2 * 48000, beta-subunit, SDS-PAGE and N-terminal sequencing
50000
-
2 * 50000, alpha-subunit, + 2 * 45000, beta subunit, + 1-3 * 11000, gamma-subunit. The gamma-subunit seems not to be an integral part of the protein
200000
-
gel filtration, both enzyme from membrane and soluble fraction
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterodimer
heterotetramer
hexamer
homotrimer
with an unprecedented fold and heme arrangement, three-dimensional structure analysis
multimer
tetramer
O33909; O33910
2 * 44200, alpha-subunit, + 2 * 41200, beta-subunit
additional information
in the CX15CH motif of heme 8, the extended region between the two cysteine residues forms a loop with a short helical turn, in direct vicinity to another loop harbouring the only non-proline cis peptide in the enzyme, between residues G508 and F509. Its formation might require the essential peptidyl isomerase MccB2, and it is presumed to be a prerequisite for correct folding of the loop in the maturation process of heme 8, which is likely to be attached by the dedicated cytochrome c synthase CcsA1. The structure of the CX15CH heme c binding motif disrupts the general parallel/perpendicular heme stacking sequence, and rotates the heme out of plane, possibly to optimize the interaction with the putative electron donor, the iron-sulfur protein MccC
heterotetramer
-
2 * 48000, alpha-subunit, 2 * 48000, beta-subunit, SDS-PAGE and N-terminal sequencing
multimer
-
2 * 50000, alpha-subunit, + 2 * 45000, beta subunit, + 1-3 * 11000, gamma-subunit. The gamma-subunit seems not to be an integral part of the protein
multimer
-
2 * 50000, alpha-subunit, + 2 * 45000, beta subunit, + 1-3 * 11000, gamma-subunit. The gamma-subunit seems not to be an integral part of the protein
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
modeling of three dimensional structure of the alpha2beta2 hetero-tetrameric protein complex
-
crystal structure at 2 A resolution and comparison with that of the phylogenetically related assimilatory sulfite reductase aSir. Dissimilatory sulfite reductase dSir is organized as a heterotetrameric complex composed of two catalytically independent alphabeta heterodimers. aSir is a monomeric protein built of two fused modules. aSir binds one siroheme-[4Fe-4S] center, dSir harbors two of them within each alphabeta heterodimer. Only one siroheme-[4Fe-4S] center in each alphabeta heterodimer is catalytically active, whereas access to the second one is blocked by a tryptophan residue
enzyme in complex with sulfite, sulfide, CO, cyanide, nitrite, nitrate, and phosphate, 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
structure of gamma-subunit DsrC, native protein to 1.12 A, and in complex with tert-butyl hydroperoxide to 2.1 A resolution. The highly conserved C-terminal arm adopts a well-defined conformation. The disulfide bond between Cys77 and Cys85 connects helices alpha3 and alpha4 and presumably plays a structural role to stabilize the protein
to 1.37 A resolution, space group P41212, with unit-cell parameters a = b = 163.26, c = 435.32 A. The crystal contains three alpha2beta2gamma2 units per asymmetric unit,
-
to 2.8 A resolution, space group P21 with unit-cell parameters a = 122.7, b = 119.4 and c = 146.7 A and b =110.0 degrees
solution structure of subunit DsrC adopts a fold consisting of an orthogonal helical bundle with a beta-hairpin along one side. The protein contains two disulfide bonds but remains folded following reduction of the disulfides. A conserved cysteine next to the C-terminus is located on a seven-residue C-terminal arm that is not part of the globular protein
purified enzyme, X-ray diffraction structure determination and analysis at 2.2 A resolution, single-wavelength anomalous dispersion
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
construction of large scale amounts of random T-DNA-inserted mutants, identification of a knockout mutant DELTAMet5. The DELTAMet5 mutant grows on sulfide but not on either sulfate or sulfite, it also grows well on Cys and homocysteine, but much slower in the presence of Met
additional information
Cryptococcus deneoformans ATCC MYA-565
-
construction of large scale amounts of random T-DNA-inserted mutants, identification of a knockout mutant DELTAMet5. The DELTAMet5 mutant grows on sulfide but not on either sulfate or sulfite, it also grows well on Cys and homocysteine, but much slower in the presence of Met
-
additional information
-
construction of large scale amounts of random T-DNA-inserted mutants, identification of a knockout mutant DELTAMet5. The DELTAMet5 mutant grows on sulfide but not on either sulfate or sulfite, it also grows well on Cys and homocysteine, but much slower in the presence of Met
-
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
DEAE Biogel column chromatography
DEAE-Biogel A column chromatography and Spherogel TSK-G-3000 gel filtration
-
DEAE-cellulose column chromatography, DEAE-Biogel A column chromatography and hydroxylapatite column chromatography
-
DEAE-Sepharose column chromatography, hydroxylapatite affinity column chromatorgaphy, Sephacryl S-400 gel filtration, and Mono-Q anion-exchange column chromatography
-
Q sepharose column chromatography
ResourceQ column chromatography, MonoBeads Q resin column chromatography Superdex 200 gel filtration, and Q Sepharose column chromatography
-
streptomycin-SO4 precipitation, alumina gel chromatography, calcium phosphate gel filtration, DEAE-cellulose column chromatography, and Sephadex G-200 gel filtration
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
Q2M487; Q2M486, Q2M485; Q2M484, Q2M483; Q2M482, Q2M481; Q2M480, Q2M479; Q2M478, Q2M476; Q2M477, Q2M475; Q2M474, Q2M472; Q2M473, Q2M471; Q2M470, Q2M468; Q2M469, Q2M466; Q2M467, Q2M464; Q2M465, Q2M463; Q2M462, Q2M460; Q2M461, Q2M459; Q2M458, Q2M456; Q2M457, Q2M455; Q2M454, Q2M453; Q2M452, Q2M451; Q2M450, Q2M449; Q2M448, Q2M446; Q2M447
gene MET5, DNA and amino acid sequence determination and analysis
structure with the alpha and beta subunits bound to the DsrC protein. The alpha2beta2gamma2 assembly contains two siroheme-[4Fe4S] cofactors bound by DsrB, two sirohydrochlorins and two [4Fe-4S]-centers bound by DsrA, and another four [4Fe-4S]-centers in the ferredoxin domains. A sulfite molecule, coordinating the siroheme, is found at the active site. The DsrC protein is bound in a cleft between DsrA and DsrB with its conserved C-terminal cysteine reaching the distal side of the siroheme. The process of sulfite reduction may involve DsrAB, DsrC, and the DsrMKJOP membrane complex (a membrane complex with putative disulfide/thiol reductase activity), in which two of the six electrons for reduction of sulfite derive from the membrane quinone pool
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Murphy, M.J.; Siegel, L.M.
Siroheme and sirohydrochlorin. The basis for a new type of porphyrin-related prosthetic group common to both assimilatory and dissimilatory sulfite reductases
J. Biol. Chem.
248
6911-6919
1973
Megalodesulfovibrio gigas, Desulfotomaculum nigrificans, Desulfotomaculum nigrificans P-582
brenda
Arendsen, A.F.; Verhagen, M.F.J.M.; Wolbert, R.B.G.; Pierik, A.J.; Stams, A.J.M.; Jetten, M.S.M.; Hagen, W.R.
The dissimilatory sulfite reductase from Desulfosarcina variabilis is a desulforubidin containing uncoupled metalated sirohemes and S = 9/2 iron-sulfur clusters
Biochemistry
32
10323-10330
1993
Desulfosarcina variabilis, Desulfosarcina variabilis DSM 2060
brenda
Seki, Y.; Nagai, Y.; Ishimoto, M.
Characterization of a dissimilatory-type sulfite reductase, desulfoviridin, from Desulfovibrio africanus Benghazi
J. Biochem.
98
1535-1543
1985
Desulfocurvibacter africanus, Desulfocurvibacter africanus Benghazi
brenda
Hatchikian, E.C.; Zeikus, J.G.
Characterization of a new type of dissimilatory sulfite reductase present in Thermodesulfobacterium commune
J. Bacteriol.
153
1211-1220
1983
Thermodesulfobacterium commune
brenda
Lui, S.M.; Cowan, J.A.
Conformational gating of the dissimilatory sulfite reductase from Desulfovibrio vulgaris (Hildenborough). Synthesis, characterization, and stopped-flow kinetics studies of 1,5-IAEDANS-labeled desulfoviridin
Biochemistry
33
11209-11216
1994
Nitratidesulfovibrio vulgaris, Nitratidesulfovibrio vulgaris Hildenborough
brenda
Steuber, J.; Arendsen, A.F.; Hagen, W.R.; Kroneck, P.M.H.
Molecular properties of the dissimilatory sulfite reductase from Desulfovibrio desulfuricans and comparison with the enzyme from Desulfovibrio vulgaris (Hildenborough)
Eur. J. Biochem.
233
873-879
1995
Desulfovibrio desulfuricans, Desulfovibrio desulfuricans Essex
brenda
Wolfe, B.M.; Lui, S.M.; Cowan, J.A.
Desulfoviridin, a multimeric-dissimilatory sulfite reductase from Desulfovibrio vulgaris (Hildenborough). Purification, characterization, kinetics and EPR studies
Eur. J. Biochem.
223
79-89
1994
Nitratidesulfovibrio vulgaris, Nitratidesulfovibrio vulgaris Hildenborough
brenda
Hall, M.H.; Prince, R.H.; Cammack, R.
EPR spectroscopy of the iron-sulphur cluster and sirohaem in the dissimilatory sulphite reductase (desulphoviridin) from Desulphovibrio gigas
Biochim. Biophys. Acta
581
27-33
1979
Megalodesulfovibrio gigas, Megalodesulfovibrio gigas 9332
brenda
Mander, G.J.; Weiss, M.S.; Hedderich, R.; Kahnt, J.; Ermler, U.; Warkentin, E.
X-ray structure of the gamma-subunit of a dissimilatory sulfite reductase: fixed and flexible C-terminal arms
FEBS Lett.
579
4600-4604
2005
Archaeoglobus fulgidus (O28055)
brenda
Schiffer, A.; Parey, K.; Warkentin, E.; Diederichs, K.; Huber, H.; Stetter, K.O.; Kroneck, P.M.; Ermler, U.
Structure of the dissimilatory sulfite reductase from the hyperthermophilic archaeon Archaeoglobus fulgidus
J. Mol. Biol.
379
1063-1074
2008
Archaeoglobus fulgidus (Q59109 and Q59110)
brenda
Oliveira, T.F.; Vonrhein, C.; Matias, P.M.; Venceslau, S.S.; Pereira, I.A.; Archer, M.
Purification, crystallization and preliminary crystallographic analysis of a dissimilatory sulfite reductase DsrAB in complex with DsrC
J. Struct. Biol.
164
236-239
2008
Nitratidesulfovibrio vulgaris (P45574), Nitratidesulfovibrio vulgaris Hildenborough (P45574)
brenda
Oliveira, T.F.; Vonrhein, C.; Matias, P.M.; Venceslau, S.S.; Pereira, I.A.; Archer, M.
The crystal structure of Desulfovibrio vulgaris dissimilatory sulfite reductase bound to DsrC provides novel insights into the mechanism of sulfate respiration
J. Biol. Chem.
283
34141-34149
2008
Nitratidesulfovibrio vulgaris (P45574 and P45575), Nitratidesulfovibrio vulgaris Hildenborough (P45574 and P45575)
brenda
Ogata, H.; Shomura, Y.; Goenka Agrawal, A.; Kaur, A.P.; Gaertner, W.; Higuchi, Y.; Lubitz, W.
Purification, crystallization and preliminary X-ray analysis of the dissimilatory sulfite reductase from Desulfovibrio vulgaris Miyazaki F
Acta Crystallogr. Sect. F
66
1470-1472
2010
Nitratidesulfovibrio vulgaris, Nitratidesulfovibrio vulgaris Miyazaki F
brenda
Moreau, J.W.; Zierenberg, R.A.; Banfield, J.F.
Diversity of dissimilatory sulfite reductase genes (dsrAB) in a salt marsh impacted by long-term acid mine drainage
Appl. Environ. Microbiol.
76
4819-4828
2010
Soil bacterium
brenda
Larsen, O.; Lien, T.; Birkeland, N.K.
Dissimilatory sulfite reductase from Archaeoglobus profundus and Desulfotomaculum thermocisternum: phylogenetic and structural implications from gene sequences
Extremophiles
3
63-70
1999
Archaeoglobus profundus (O93650 and O93651), Archaeoglobus profundus DSM 5631 (O93650 and O93651), Desulfofundulus thermocisternus (Q9ZH18 and Q9ZH17)
brenda
Holkenbrink, C.; Barbas, S.O.; Mellerup, A.; Otaki, H.; Frigaard, N.U.
Sulfur globule oxidation in green sulfur bacteria is dependent on the dissimilatory sulfite reductase system
Microbiology
157
1229-1239
2011
Chlorobaculum tepidum (Q8K5E9), Chlorobaculum tepidum DSM 12025 (Q8K5E9)
brenda
Ghosh, S.; Bagchi, A.
Intermolecular interaction study of dissimilatory sulfite reductase (DsrAB) from sulfur oxidizing proteobacteria Allchromatium vinosum
AIDS Res. Hum. Retroviruses
340
19-27
2015
Allochromatium vinosum
-
brenda
Marritt, S.J.; Hagen, W.F.
Dissimilatory sulfite reductase revisited. The desulfoviridin molecule does contain 20 iron ions, extensively demetallated sirohaem, and an S = 9/2 iron-sulfur cluster
Eur. J. Biochem.
238
724-727
1996
Nitratidesulfovibrio vulgaris
brenda
Cort, J.R.; Mariappan, S.V.; Kim, C.Y.; Park, M.S.; Peat, T.S.; Waldo, G.S.; Terwilliger, T.C.; Kennedy, M.A.
Solution structure of Pyrobaculum aerophilum DsrC, an archaeal homologue of the gamma subunit of dissimilatory sulfite reductase
Eur. J. Biochem.
268
5842-5850
2001
Pyrobaculum aerophilum (Q8ZUX1), Pyrobaculum aerophilum DSM 7523 (Q8ZUX1)
brenda
Pott, A.; Dahl, C.
Sirohaem sulfite reductase and other proteins encoded by genes at the dsr locus of Chromatium vinosum are involved in the oxidation of intracellular sulfur
Microbiology
144
1881-1894
1998
Allochromatium vinosum (O33998 and D3RSN2), Allochromatium vinosum DSM 180 (O33998 and D3RSN2)
-
brenda
Molitor, M.; Dahl, C.; Molitor, I.; Schaefer, U.; Speich, N.; Huber, R.; Deutzmann, R.; Trueper, H.G.
A dissimilatory sirohaem-sulfite-reductase-type protein from the hyperthermophilic archaeon Pyrobaculum islandicum
Microbiology
144
529-541
1998
Pyrobaculum islandicum (O33909 and O33910)
brenda
Mori, Y.; Kataoka, T.; Okamura, T.; Kondo, R.
Dominance of green sulfur bacteria in the chemocline of the meromictic Lake Suigetsu, Japan, as revealed by dissimilatory sulfite reductase gene analysis
Arch. Microbiol.
195
303-312
2013
Candidatus Ruthturnera calyptogenae, Candidatus Thiobius zoothamnicola, Chlorobium limicola, Chlorobium phaeovibrioides, Halochromatium salexigens, Magnetospirillum gryphiswaldense, Pelodictyon luteolum
brenda
Venceslau, S.S.; Cort, J.R.; Baker, E.S.; Chu, R.K.; Robinson, E.W.; Dahl, C.; Saraiva, L.M.; Pereira, I.A.
Redox states of Desulfovibrio vulgaris DsrC, a key protein in dissimilatory sulfite reduction
Biochem. Biophys. Res. Commun.
441
732-736
2013
Nitratidesulfovibrio vulgaris
brenda
Duarte, A.G.; Santos, A.A.; Pereira, I.A.
Electron transfer between the QmoABC membrane complex and adenosine 5-phosphosulfate reductase
Biochim. Biophys. Acta
1857
380-386
2016
Desulfovibrio desulfuricans
brenda
Leavitt, W.D.; Bradley, A.S.; Santos, A.A.; Pereira, I.A.; Johnston, D.T.
Sulfur isotope effects of dissimilatory sulfite reductase
Front. Microbiol.
6
1392
2015
Archaeoglobus fulgidus, Nitratidesulfovibrio vulgaris, Nitratidesulfovibrio vulgaris DSM 644
brenda
Lee, J.; Kim, B.; Ki, M.
Construction of aligned database of dsrA, a gene encoding dissimilatory sulfite reductase alpha subunit, for metagenomic studies of sulfate-reducing bacteria
J. Korean Soc. Appl. Biol. Chem.
57
419-427
2014
Chlorobium phaeobacteroides, Chlorobium phaeobacteroides BS1, Chlorobium phaeobacteroides DSM 266, Desulfitobacterium dichloroeliminans, Desulfitobacterium dichloroeliminans LMG P-21439, Desulfosporosinus orientis, Desulfosporosinus orientis DSM 765, Nitratidesulfovibrio vulgaris, Nitratidesulfovibrio vulgaris DP4, Nitratidesulfovibrio vulgaris Hildenborough, Thermaerobacter marianensis, Thermaerobacter marianensis AB011495
-
brenda
Hermann, B.; Kern, M.; La Pietra, L.; Simon, J.; Einsle, O.
The octahaem MccA is a haem c-copper sulfite reductase
Nature
520
706-709
2015
Wolinella succinogenes (Q7MSJ8)
brenda
Nguyen, P.T.; Toh-E, A.; Nguyen, N.H.; Imanishi-Shimizu, Y.; Watanabe, A.; Kamei, K.; Shimizu, K.
Identification and characterization of a sulfite reductase gene and new insights regarding the sulfur-containing amino acid metabolism in the basidiomycetous yeast Cryptococcus neoformans
Curr. Genet.
67
115-128
2021
Cryptococcus deneoformans (Q5K8J1), Cryptococcus deneoformans ATCC MYA-565 (Q5K8J1), Cryptococcus deneoformans JEC21 (Q5K8J1)
brenda
Moura, I.; Lino, A.R.; Moura, J.J.; Xavier, A.V.; Fauque, G.; Peck, H.D. Jr.; LeGall, J.
Low-spin sulfite reductases a new homologous group of non-heme iron-siroheme proteins in anaerobic bacteria
Biochem. Biophys. Res. Commun.
141
1032-1041
1986
Desulfuromonas acetoxidans, Desulfuromonas acetoxidans 5071, Methanosarcina barkeri, Methanosarcina barkeri DSM 800
brenda
Parey, K.; Warkentin, E.; Kroneck, P.M.; Ermler, U.
Reaction cycle of the dissimilatory sulfite reductase from Archaeoglobus fulgidus
Biochemistry
49
8912-8921
2010
Archaeoglobus fulgidus (Q59109 and Q59110)
brenda
Venceslau, S.S.; Stockdreher, Y.; Dahl, C.; Pereira, I.A.
The ''bacterial heterodisulfide'' DsrC is a key protein in dissimilatory sulfur metabolism
Biochim. Biophys. Acta
1837
1148-1164
2014
Allochromatium vinosum, Caldivirga maquilingensis, Carboxydothermus hydrogenoformans, Desulfitobacterium dehalogenans, Desulfitobacterium dichloroeliminans, Desulfitobacterium hafniense, Desulfofarcimen acetoxidans, Desulfofundulus kuznetsovii, Desulfonispora thiosulfatigenes, Desulfotalea psychrophila, Desulfovibrio desulfuricans, Desulfovirgula thermocuniculi, Neomoorella thermoacetica, Nitratidesulfovibrio vulgaris (P45574 and P45575), Syntrophobacter fumaroxidans, Thermanaeromonas toyohensis, Thermodesulfobacterium thermophilum, Thermodesulfobium narugense, Thermosinus carboxydivorans
brenda
Loy, A.; Duller, S.; Baranyi, C.; Mussmann, M.; Ott, J.; Sharon, I.; Beja, O.; Le Paslier, D.; Dahl, C.; Wagner, M.
Reverse dissimilatory sulfite reductase as phylogenetic marker for a subgroup of sulfur-oxidizing prokaryotes
Environ. Microbiol.
11
289-299
2009
Alkalilimnicola ehrlichii, Alkalilimnicola ehrlichii MLHE1, Allochromatium vinosum, Allochromatium vinosum U84760, bacterium, Candidatus Ruthturnera calyptogenae, Candidatus Ruthturnera calyptogenae Cm, Candidatus Vesicomyidisocius calyptogenae, Candidatus Vesicomyidisocius calyptogenae HA, Chlorobaculum tepidum, Chlorobaculum tepidum TLS, Chlorobium chlorochromatii, Chlorobium chlorochromatii CaD3, Chlorobium limicola, Chlorobium limicola DSM 245, Chlorobium phaeobacteroides, Chlorobium phaeobacteroides BS1, Chlorobium phaeovibrioides, Chlorobium phaeovibrioides DSM 265, Halorhodospira halophila, Halorhodospira halophila SL1, Magnetococcus marinus MC-1, Paramagnetospirillum magnetotacticum, Paramagnetospirillum magnetotacticum MS-1, Pelodictyon clathratiforme, Pelodictyon clathratiforme BU-1, Pelodictyon luteolum, Pelodictyon luteolum DSM 273, Prosthecochloris aestuarii, Prosthecochloris aestuarii DSM 271, Thiobacillus denitrificans, uncultured bacterium BAC13K9BAC
brenda
Loeffler, M.; Feldhues, J.; Venceslau, S.S.; Kammler, L.; Grein, F.; Pereira, I.A.C.; Dahl, C.
DsrL mediates electron transfer between NADH and rDsrAB in Allochromatium vinosum
Environ. Microbiol.
22
783-795
2020
Allochromatium vinosum
brenda
Ferreira, D.; Venceslau, S.S.; Bernardino, R.; Preto, A.; Zhang, L.; Waldbauer, J.R.; Leavitt, W.D.; Pereira, I.A.C.
DsrC is involved in fermentative growth and interacts directly with the FlxABCD-HdrABC complex in Desulfovibrio vulgaris Hildenborough
Environ. Microbiol.
25
962-976
2023
Nitratidesulfovibrio vulgaris (P45574 and P45575)
brenda
Perez-Jimenez, J.R.; Young, L.Y.; Kerkhof, L.J.
Molecular characterization of sulfate-reducing bacteria in anaerobic hydrocarbon-degrading consortia and pure cultures using the dissimilatory sulfite reductase (dsrAB) genes
FEMS Microbiol. Ecol.
35
145-150
2001
Desulfosudis oleivorans (Q93TS0), Desulfosudis oleivorans DSM 6200 (Q93TS0), Desulfovibrio sp. TBP-1 (Q93TS1), sulfate-reducing bacterium AK-01 (Q93TS8 AND Q93TS7), sulfate-reducing bacterium STC (Q93TQ5), uncultured bacterium BMNP (Q93TS6), uncultured benzene mineralizing bacterium (Q93TS4), uncultured benzene mineralizing bacterium (Q93TS3), uncultured benzene mineralizing bacterium (Q93TS2), uncultured napthalene mineralizing bacterium (Q93TR8), uncultured napthalene mineralizing bacterium (Q93TR7), uncultured napthalene mineralizing bacterium (Q93TR6), uncultured napthalene mineralizing bacterium (Q93TR9), uncultured napthalene mineralizing bacterium (Q93TR5), uncultured phenanthrene mineralizing bacterium (Q93TR4), uncultured phenanthrene mineralizing bacterium (Q93TR3), uncultured phenanthrene mineralizing bacterium (Q93TR2), uncultured phenanthrene mineralizing bacterium (Q93TR1), uncultured phenanthrene mineralizing bacterium (Q93TR0), uncultured phenanthrene mineralizing bacterium (Q93TQ9), uncultured phenanthrene mineralizing bacterium (Q93TQ8), uncultured phenanthrene mineralizing bacterium (Q93TQ7), uncultured phenanthrene mineralizing bacterium (Q93TQ6)
brenda
Leloup, J.; Quillet, L.; Berthe, T.; Petit, F.
Diversity of the dsrAB (dissimilatory sulfite reductase) gene sequences retrieved from two contrasting mudflats of the Seine estuary, France
FEMS Microbiol. Ecol.
55
230-238
2006
uncultured sulfate-reducing bacterium (Q2M487 AND Q2M486), uncultured sulfate-reducing bacterium (Q2M485 AND Q2M484), uncultured sulfate-reducing bacterium (Q2M483 AND Q2M482), uncultured sulfate-reducing bacterium (Q2M481 AND Q2M480), uncultured sulfate-reducing bacterium (Q2M479 AND Q2M478), uncultured sulfate-reducing bacterium (Q2M476 AND Q2M477), uncultured sulfate-reducing bacterium (Q2M475 AND Q2M474), uncultured sulfate-reducing bacterium (Q2M472 AND Q2M473), uncultured sulfate-reducing bacterium (Q2M471 AND Q2M470), uncultured sulfate-reducing bacterium (Q2M468 AND Q2M469), uncultured sulfate-reducing bacterium (Q2M466 AND Q2M467), uncultured sulfate-reducing bacterium (Q2M464 AND Q2M465), uncultured sulfate-reducing bacterium (Q2M463 AND Q2M462), uncultured sulfate-reducing bacterium (Q2M460 AND Q2M461), uncultured sulfate-reducing bacterium (Q2M459 AND Q2M458), uncultured sulfate-reducing bacterium (Q2M456 AND Q2M457), uncultured sulfate-reducing bacterium (Q2M455 AND Q2M454), uncultured sulfate-reducing bacterium (Q2M453 AND Q2M452), uncultured sulfate-reducing bacterium (Q2M451 AND Q2M450), uncultured sulfate-reducing bacterium (Q2M449 AND Q2M448), uncultured sulfate-reducing bacterium (Q2M446 AND Q2M447)
brenda
Larsen, O.; Lien, T.; Birkeland, N.K.
A novel organization of the dissimilatory sulfite reductase operon of Thermodesulforhabdus norvegica verified by RT-PCR
FEMS Microbiol. Lett.
203
81-85
2001
Thermodesulforhabdus norvegica
brenda
Huynh, B.; Moura, I.; Lino, A.; Moura, J.; Legall, J.
Characterization of two dissimilatory sulfite reductases from sulfate-reducing bacteria
Hyperfine Interact.
42
905-908
1988
Megalodesulfovibrio gigas, Desulfomicrobium baculatum, Desulfomicrobium baculatum DSM 1743
-
brenda
Steuber, J.; Kroneck, P.
Desulfoviridin, the dissimilatory sulfite reductase from Desulfovibrio desulfuricans (Essex) New structural and functional aspects of the membranous enzyme
Inorg. Chim. Acta
275-276
52-57
1998
Desulfovibrio desulfuricans, Desulfovibrio desulfuricans DSM 642
-
brenda
Mueller, A.L.; Kjeldsen, K.U.; Rattei, T.; Pester, M.; Loy, A.
Phylogenetic and environmental diversity of DsrAB-type dissimilatory (bi)sulfite reductases
ISME J.
9
1152-1165
2015
Allochromatium vinosum, Azospirillum halopraeferens, Candidatus Riegeria paracatenulae, Candidatus Ruthturnera calyptogenae, Candidatus Ruthturnera calyptogenae Cm, Candidatus Vesicomyidisocius calyptogenae, Candidatus Vesicomyidisocius calyptogenae HA, Chlorobaculum parvum, Chlorobaculum tepidum, Chlorobium chlorochromatii, Chlorobium chlorochromatii CaD3, Chlorobium limicola, Chlorobium phaeobacteroides, Chlorobium phaeovibrioides, Halochromatium salexigens, Halorhodospira halophila, Lamprocystis purpurea, Magnetococcus marinus, Magnetospirillum gryphiswaldense, Marichromatium gracile, Marichromatium purpuratum, Neomoorella thermoacetica, Nitratidesulfovibrio vulgaris (P45574 and P45575), Paramagnetospirillum caucaseum, Paramagnetospirillum magneticum, Paramagnetospirillum magnetotacticum, Paramagnetospirillum magnetotacticum MS-1, Pelodictyon clathratiforme, Pelodictyon luteolum, Prosthecochloris aestuarii, Prosthecochloris vibrioformis, Rhodomicrobium vannielii, Sedimenticola selenatireducens, Sideroxydans lithotrophicus, Sulfuricella denitrificans, Thioalkalivibrio nitratireducens, Thioalkalivibrio paradoxus, Thioalkalivibrio sulfidiphilus, Thioalkalivibrio thiocyanodenitrificans, Thiobaca trueperi, Thiobacillus denitrificans, Thiobacillus thioparus, Thiocapsa marina, Thiocapsa rosea, Thiocapsa roseopersicina, Thiocystis gelatinosa, Thiocystis violacea, Thiocystis violascens, Thiofilum flexile, Thioflavicoccus mobilis, Thiolinea disciformis, Thiorhodococcus drewsii, Thiorhodovibrio frisius, Thiothrix nivea, Allochromatium vinosum DSM 180, Azospirillum halopraeferens DSM 3675, Chlorobaculum tepidum DSM 12025, Chlorobium limicola DSM 245, Chlorobium phaeobacteroides BS1, Chlorobium phaeobacteroides DSM 266, Chlorobium phaeovibrioides DSM 265, Halochromatium salexigens DSM 4395, Halorhodospira halophila DSM 244, Lamprocystis purpurea DSM 4197, Magnetospirillum gryphiswaldense DSM 6361, Marichromatium gracile DSM 203, Marichromatium purpuratum DSM 1591, Nitratidesulfovibrio vulgaris DSM 644 (P45574 and P45575), Paramagnetospirillum magneticum AMB-1, Pelodictyon clathratiforme DSM 5477, Prosthecochloris aestuarii DSM 271, Rhodomicrobium vannielii DSM 162, Sedimenticola selenatireducens DSM 17993, Sideroxydans lithotrophicus ES-1, Sulfuricella denitrificans DSM 22764, Thioalkalivibrio nitratireducens DSM 14787, Thioalkalivibrio paradoxus ARh1, Thioalkalivibrio sulfidiphilus HL-EbGr7, Thioalkalivibrio thiocyanodenitrificans DSM 16954, Thiobaca trueperi DSM 13587, Thiobacillus denitrificans DSM 12475, Thiobacillus thioparus DSM 505, Thiocapsa marina DSM 5653, Thiocapsa rosea DSM 235, Thiocapsa roseopersicina M11, Thiocystis gelatinosa DSM 215, Thiocystis violacea DSM 208, Thiocystis violascens DSM 198, Thiofilum flexile DSM 14609, Thioflavicoccus mobilis 8321, Thiolinea disciformis DSM 14473, Thiorhodococcus drewsii DSM 15006, Thiothrix nivea DSM 5205, Candidatus Riegeria paracatenulae C08085, Chlorobaculum parvum NCIB 8327, Chlorobium phaeovibrioides DSM 269, Pelodictyon luteolum DSM 273, Prosthecochloris vibrioformis DSM 261
brenda
Legall, J.; Peck, H.; Dervartanian, D.; Moura, I.; Lino, A.; Xavier, A.; Moura, J.; Fauque, G.; Huynh, B.
Characterization of two dissimilatory sulfite reductases (desulforubidin and desulfoviridin) from the sulfate-reducing bacteria. Mossbauer and EPR studies
J. Am. Chem. Soc.
110
1075-1082
1988
Megalodesulfovibrio gigas, Desulfomicrobium baculatum, Desulfomicrobium baculatum DSM 1743
-
brenda
Lui, S.; Liang, W.; Soriano, A.; Cowan, J.
Enzymatic reduction of inorganic anions. Variable-temperature steady-state and pre-steady-state kinetics experiments to map the energy profile of an enzymatic multielectron redox reaction. Application to the dissimilatory sulfite reductase from Desulfovibrio vulgaris (Hildenborough)
J. Am. Chem. Soc.
116
4531-4536
1994
Nitratidesulfovibrio vulgaris, Nitratidesulfovibrio vulgaris NCIB 8303
-
brenda
Lee, J.; LeGall, J.; Peck Jr, H.
Isolation of assimilatory- and dissimilatory type sulfite reductases from Desulfovibrio vulgaris
J. Bacteriol.
115
529-542
1973
Nitratidesulfovibrio vulgaris, Nitratidesulfovibrio vulgaris NCIB 8303
brenda
Seki, Y.; Sogawa, N.; Ishimoto, M.
Siroheme as an active catalyst in sulfite reduction
J. Biochem.
90
1487-1492
1981
Megalodesulfovibrio gigas
brenda
Cort, J.R.; Selan, U.; Schulte, A.; Grimm, F.; Kennedy, M.A.; Dahl, C.
Allochromatium vinosum DsrC solution-state NMR structure, redox properties, and interaction with DsrEFH, a protein essential for purple sulfur bacterial sulfur oxidation
J. Mol. Biol.
382
692-707
2008
Allochromatium vinosum
brenda
Ferreira, D.; Barbosa, A.C.C.; Oliveira, G.P.; Catarino, T.; Venceslau, S.S.; Pereira, I.A.C.
The DsrD functional marker protein is an allosteric activator of the DsrAB dissimilatory sulfite reductase
Proc. Natl. Acad. Sci. USA
119
e2118880119
2022
Archaeoglobus fulgidus (Q59109 and Q59110)
brenda
Colman, D.; Labesse, G.; Swapna, G.; Stefanakis, J.; Montelione, G.; Boyd, E.; Royer, C.
Structural evolution of the ancient enzyme, dissimilatory sulfite reductase
Proteins Struct. Funct. Bioinform.
90
1331-1345
2022
Nitratidesulfovibrio vulgaris (P45574 and P45575), Archaeoglobus fulgidus (Q59109 and Q59110), Nitratidesulfovibrio vulgaris DSM 644 (P45574 and P45575)
brenda
Santos, A.; Venceslau, S.; Grein, F.; Leavitt, W.; Dahl, C.; Johnston, D.; Pereira, I.
A protein trisulfide couples dissimilatory sulfate reduction to energy conservation
Science
350
1541-1545
2015
Archaeoglobus fulgidus (Q59109 and Q59110)
brenda
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