CATH Classification

Domain Context

CATH Clusters

Superfamily DsrC-like protein, C-terminal domain
Functional Family

Enzyme Information

1.8.99.5
Dissimilatory sulfite reductase.
based on mapping to UniProt P45573
(1) Hydrogen sulfide + a [DsrC protein]-disulfide + 2 acceptor + 3 H(2)O = sulfite + a [DsrC protein]-dithiol + 2 reduced acceptor + 2 H(+). (2) A [DsrC protein]-S-sulfanyl-L-cysteine + 3 acceptor + 3 H(2)O = sulfite + a [DsrC protein]-disulfide + 3 reduced acceptor + 2 H(+).
-!- 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 catalyzes the reduction of sulfite to sulfide, while in sulfur oxidizers it catalyzes the opposite reaction. -!- 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. -!- This enzyme is different from EC 1.8.1.2 and EC 1.8.7.1, which are involved in sulfate assimilation.

UniProtKB Entries (1)

P45574
DSVA_DESVH
Desulfovibrio vulgaris str. Hildenborough
Sulfite reductase, dissimilatory-type subunit alpha

PDB Structure

PDB 2V4J
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
The Crystal Structure of Desulfovibrio Vulgaris Dissimilatory Sulfite Reductase Bound to Dsrc Provides Novel Insights Into the Mechanism of Sulfate Respiration.
Oliveira, T.F., Vonrhein, C., Matias, P.M., Venceslau, S.S., Pereira, I.A.C., Archer, M.
J.Biol.Chem.
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