1.8.99.5: dissimilatory sulfite reductase
This is an abbreviated version!
For detailed information about dissimilatory sulfite reductase, go to the full flat file.
Word Map on EC 1.8.99.5
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1.8.99.5
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sulfate-reducing
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desulfovibrio
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thiosulfate
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sulfur-oxidizing
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biogeochemical
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desulfobacteraceae
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geochemical
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vinosum
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desulfotomaculum
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allochromatium
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phylotypes
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adenosine-5'-phosphosulfate
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desulfoviridin
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desulfobulbus
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desulfosarcina
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hildenborough
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desulfobulbaceae
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chemotrophic
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desulfovibrionaceae
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low-sulfate
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sulfidogenic
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aarhus
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deltaproteobacterial
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chlorobaculum
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methane-oxidizing
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hydrogenotrophic
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desulfobacterium
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desulfomicrobium
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sirohaem
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desulfococcus
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t-rflp
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desulfosporosinus
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anme-2
- 1.8.99.5
-
sulfate-reducing
- desulfovibrio
- thiosulfate
-
sulfur-oxidizing
-
biogeochemical
- desulfobacteraceae
-
geochemical
- vinosum
- desulfotomaculum
- allochromatium
-
phylotypes
- adenosine-5'-phosphosulfate
-
desulfoviridin
- desulfobulbus
- desulfosarcina
- hildenborough
- desulfobulbaceae
-
chemotrophic
- desulfovibrionaceae
-
low-sulfate
-
sulfidogenic
-
aarhus
-
deltaproteobacterial
- chlorobaculum
-
methane-oxidizing
-
hydrogenotrophic
- desulfobacterium
- desulfomicrobium
-
sirohaem
- desulfococcus
-
t-rflp
- desulfosporosinus
-
anme-2
Reaction
+ 2 acceptor + 3 H2O = + + 2 reduced acceptor + 2 H+
Synonyms
CNL05500, dSiR, DsrA, DsrAB, DsrC, DsvA, DsvB, hydrogen-sulfide:(acceptor) oxidoreductase, MET5, octahaemcytochrome c MccA, PAE2566, SiRA, siroheme sulfite reductase, sulfite reductase
ECTree
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Crystallization
Crystallization on EC 1.8.99.5 - dissimilatory sulfite reductase
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modeling of three dimensional structure 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
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
purified enzyme, X-ray diffraction structure determination and analysis at 2.2 A resolution, single-wavelength anomalous dispersion