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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Subunits
Subunits on EC 1.8.99.5 - dissimilatory sulfite reductase
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heterodimer
heterotetramer
homotrimer
with an unprecedented fold and heme arrangement, three-dimensional structure analysis
multimer
tetramer
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
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2 * 48000, alpha-subunit, 2 * 48000, beta-subunit, SDS-PAGE and N-terminal sequencing
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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
multimer
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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
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