Information on EC 1.8.99.5 - dissimilatory sulfite reductase

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

EC NUMBER
COMMENTARY hide
1.8.99.5
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RECOMMENDED NAME
GeneOntology No.
dissimilatory sulfite reductase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a [DsrC protein]-S-sulfanyl-L-cysteine + 2 acceptor + 3 H2O = sulfite + a [DsrC protein]-dithiol + 2 reduced acceptor + 2 H+
show the reaction diagram
(1b)
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-
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a [DsrC protein]-S-sulfanyl-L-cysteine + 3 acceptor + 3 H2O = a [DsrC]-S-sulfo-L-cysteine + 3 reduced acceptor + H+
show the reaction diagram
(2a)
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-
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a [DsrC protein]-S-sulfanyl-L-cysteine + 3 acceptor + 3 H2O = sulfite + a [DsrC protein]-disulfide + 3 reduced acceptor + 2 H+
show the reaction diagram
(2), overall reaction
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a [DsrC]-S-sulfo-L-cysteine = sulfite + a [DsrC protein]-disulfide
show the reaction diagram
(2b)
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hydrogen sulfide + a [DsrC protein]-disulfide + 2 acceptor + 3 H2O = sulfite + a [DsrC protein]-dithiol + 2 reduced acceptor + 2 H+
show the reaction diagram
(1), overall reaction
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hydrogen sulfide + a [DsrC protein]-disulfide = a [DsrC protein]-S-sulfanyl-L-cysteine
show the reaction diagram
(1a)
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Metabolic pathways
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Microbial metabolism in diverse environments
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Nitrotoluene degradation
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sulfate reduction IV (dissimilatory, to hydrogen sufide))
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sulfate reduction V (dissimilatory, to thiosulfate)
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Sulfur metabolism
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superpathway of tetrathionate reduction (Salmonella typhimurium)
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superpathway of thiosulfate metabolism (Desulfovibrio sulfodismutans)
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non-pathway related
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SYSTEMATIC NAME
IUBMB Comments
hydrogen-sulfide:[DsrC sulfur-carrier protein],acceptor oxidoreductase
Contain siroheme. The enzyme is essential in prokaryotic sulfur-based energy metabolism, including sulfate/sulfite reducing organisms, sulfur-oxidizing bacteria, and organosulfonate reducers. In sulfur reducers it catalyses the reduction of sulfite to sulfide (reaction 1 in the right to left direction), while in sulfur oxidizers it catalyses the opposite reaction (reaction 2 in the left to right direction) [1]. The reaction involves the small protein DsrC, which is present in all the organisms that contain dissimilatory sulfite reductase. During the process an intramolecular disulfide bond is formed between two L-cysteine residues of DsrC. This disulfide can be reduced by a number of proteins including DsrK and TcmB [5]. This enzyme is different from EC 1.8.1.2, assimilatory sulfite reductase (NADPH), and EC 1.8.7.1, assimilatory sulfite reductase (ferredoxin), which are involved in sulfate assimilation.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
O33998, i.e. subunit DsrA, D3RSN2 i.e. subunit DsrB
O33998 and D3RSN2
UniProt
Manually annotated by BRENDA team
O93650 i.e. subunit DsrA, O93651 i.e. subunit DsrB
O93650 and O93651
UniProt
Manually annotated by BRENDA team
O93650 i.e. subunit DsrA, O93651 i.e. subunit DsrB
O93650 and O93651
UniProt
Manually annotated by BRENDA team
Q9ZH18 i.e. subunit DsrA, Q9ZH17 i.e. subunit DsrB
Q9ZH18 and Q9ZH17
UniProt
Manually annotated by BRENDA team
subunit DsrC
UniProt
Manually annotated by BRENDA team
subunit DsrC
UniProt
Manually annotated by BRENDA team
O33909 i.e. subunit DsrA, O33910 i.e. subunit DsrB
O33909 and O33910
UniProt
Manually annotated by BRENDA team
Soil bacterium
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
hydroxylamine + a [DsrC protein]-dithiol + 2 reduced acceptor + 2 H+
? + a [DsrC protein]-disulfide + 2 acceptor + 3 H2O
show the reaction diagram
nitrite + a [DsrC protein]-dithiol + 2 reduced acceptor
? + a [DsrC protein]-disulfide + 2 acceptor + 2 H2O
show the reaction diagram
SeO32- + a [DsrC protein]-dithiol + 2 reduced methyl viologen + 2 H+
HSe- + a [DsrC protein]-disulfide + 2 oxidized methyl viologen + 3 H2O
show the reaction diagram
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40% of the activity with sulfite
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?
sulfite + a [DsrC protein]-dithiol + 2 reduced ferredoxin + 2 H+
hydrogen sulfide + a [DsrC protein]-disulfide + 2 oxidized ferredoxin + 3 H2O
show the reaction diagram
sulfite + a [DsrC protein]-dithiol + reduced methyl viologen
trithionate + a [DsrC protein]-disulfide + oxidized methyl viologen
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
siroheme
[4Fe-4S]-center
additional information
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no activity is observed with NAD, NADP, FAD or FMN
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KCN
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1 mM, complete inhibition
NaN3
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1 mM, 18% inhibition
Tris/HCl
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Tris buffer has an inhibitory effect. Approximately 60% less activity than with phosphate buffer is obtained at pH 7.5
additional information
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not inhibitory: iodoacetate
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
48
hydroxylamine
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pH 7.6, 22°C
0.028
nitrite
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pH 7.6, 22°C
0.06 - 3.1
sulfite
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
29
hydroxylamine
Desulfovibrio vulgaris
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pH 7.6, 22°C
0.038
nitrite
Desulfovibrio vulgaris
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pH 7.6, 22°C
0.31
sulfite
Desulfovibrio vulgaris
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pH 7.6, 22°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.6
hydroxylamine
Desulfovibrio vulgaris
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pH 7.6, 22°C
85
1.4
nitrite
Desulfovibrio vulgaris
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pH 7.6, 22°C
168
5.17
sulfite
Desulfovibrio vulgaris
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pH 7.6, 22°C
92
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
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phosphate buffer
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.3
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isoelectric focusing
8.4
O33909 and O33910
isoelectric focusing
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Desulfomicrobium norvegicum (strain DSM 1741 / NCIMB 8310)
Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / DSM 644 / NCIMB 8303)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
11000
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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
12700
x * 12700, subunit DsrC, claculated
13400
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2 * 13400 plus 2 * 28400, SDS-PAGE
28400
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2 * 13400 plus 2 * 28400, SDS-PAGE
41200
O33909 and O33910
2 * 44200, alpha-subunit, + 2 * 41200, beta-subunit
44200
O33909 and O33910
2 * 44200, alpha-subunit, + 2 * 41200, beta-subunit
45000
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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
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2 * 48000, alpha-subunit, 2 * 48000, beta-subunit, SDS-PAGE and N-terminal sequencing
50000
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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
165000
O33909 and O33910
PAGE
167000
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sedimentation equilibrium centrifugation
170000
O33909 and O33910
gel filtration
200000
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gel filtration, both enzyme from membrane and soluble fraction
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterotetramer
multimer
tetramer
O33909 and O33910
2 * 44200, alpha-subunit, + 2 * 41200, beta-subunit
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
modeling of three dimensional strucuture of the alpha2beta2 hetero-tetrameric protein complex
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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
Q59109 and Q59110
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,
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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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70
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stable up to, rapidly denatures above
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
both from membrane and soluble fraction
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Q59109 and Q59110
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
P45574 and P45575