CATH Classification
Level | CATH Code | Description |
---|---|---|
1 | Mainly Alpha | |
1.10 | Orthogonal Bundle | |
1.10.10 | Arc Repressor Mutant, subunit A | |
1.10.10.370 | DsrC-like protein, C-terminal domain |
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.
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UniProtKB Entries (1)
P45574 |
DSVA_DESVH
Desulfovibrio vulgaris str. Hildenborough
Sulfite reductase, dissimilatory-type subunit alpha
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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.
J.Biol.Chem.
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