| Entry |
|
| Name |
dissimilatory sulfite reductase;
siroheme sulfite reductase;
hydrogen-sulfide:(acceptor) oxidoreductase (ambiguous);
DsrAB
|
| Class |
Oxidoreductases;
Acting on a sulfur group of donors;
With unknown physiological acceptors
 |
| Sysname |
hydrogen-sulfide:[DsrC sulfur-carrier protein],acceptor oxidoreductase
|
| Reaction(IUBMB) |
(1) hydrogen sulfide + a [DsrC protein]-disulfide + 2 acceptor + 3 H2O = sulfite + a [DsrC protein]-dithiol + 2 reduced acceptor + 2 H+ (overall reaction);
(1a) hydrogen sulfide + a [DsrC protein]-disulfide = a [DsrC protein]-S-sulfanyl-L-cysteine;
(1b) a [DsrC protein]-S-sulfanyl-L-cysteine + 2 acceptor + 3 H2O = sulfite + a [DsrC protein]-dithiol + 2 reduced acceptor + 2 H+;
(2) a [DsrC protein]-S-sulfanyl-L-cysteine + 3 acceptor + 3 H2O = sulfite + a [DsrC protein]-disulfide + 3 reduced acceptor + 2 H+ (overall reaction);
(2a) a [DsrC protein]-S-sulfanyl-L-cysteine + 3 acceptor + 3 H2O = a [DsrC]-S-sulfo-L-cysteine + 3 reduced acceptor + H+;
(2b) a [DsrC]-S-sulfo-L-cysteine = sulfite + a [DsrC protein]-disulfide
|
| Reaction(KEGG) |
|
| Substrate |
hydrogen sulfide [CPD: C00283];
[DsrC protein]-disulfide;
acceptor [CPD: C00028];
H2O [CPD: C00001];
[DsrC protein]-S-sulfanyl-L-cysteine;
[DsrC]-S-sulfo-L-cysteine
|
| Product |
sulfite [CPD: C00094];
[DsrC protein]-dithiol;
reduced acceptor [CPD: C00030];
H+ [CPD: C00080];
[DsrC protein]-S-sulfanyl-L-cysteine;
[DsrC protein]-disulfide;
[DsrC]-S-sulfo-L-cysteine
|
| Comment |
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.
|
| History |
EC 1.8.99.5 created 2015
|
| Pathway |
| Nitrotoluene degradation | | Sulfur metabolism | | Metabolic pathways | | Microbial metabolism in diverse environments |
|
| Orthology |
| dissimilatory sulfite reductase alpha subunit | | dissimilatory sulfite reductase beta subunit |
|
| Genes |
TIG: | | ALV: | | TVI: | | TMB: | | MPUR: | | AEH: | | HHA: | | TGR: | | TNI: | | TTI: | | TBN: | | SEDS: | | THO: | | RMA: | | VOK: | | EBH: | | ENM: | | BBAG: | | SHD: | | TBD: | | SLT: | | SDR: | | DVU: | | DVL: | | DVM: | | DVG: | | DDE: | | DDS: | | DDN: | | DMA: | | DSA: | | DAS: | | DAF: | | DHY: | | DPI: | | DGG: | | DFI: | | DEJ: | | DPG: | | DBA: | | DOA: | | DRT: | | DPS: | | DAK: | | DPR: | | DSF: | | DOL: | | DML: | | DAL: | | DAT: | | DTO: | | DAO: | | DTI: | | SFU: | | DBR: | | DAV: | | RVA: | | MAG: | | MGY: | | MAGX: | | MAGN: | | MAGQ: | | MGM: | | DSY: | | DHD: | | DDH: | | DDL: | | DRM: | | DAE: | | DCA: | | DKU: | | DRU: | | DGI: | | DFG: | | DAU: | | DOR: | | DAI: | | DMI: | | CHY: | | MTA: | | ADG: | | TNR: | | GPA: | | CBAC: | | CTE: | | CPC: | | CLZ: | | CCH: | | CPH: | | CPB: | | CLI: | | PVI: | | PLT: | | PPH: | | PAA: | | PROC: | | PRS: | | TYE: | | TID: | | TOP: | | TCM: | | CTHI: | | AFU: | | AFG: | | APO: | | AVE: | | AST: | | PAI: | | PIS: | | PCL: | | PAS: | | PYR: | | POG: | | TNE: | | CMA: | | TTN: | | VDI: | | VMO: | | » show all
 |
| Reference |
1 |
| Authors |
Schedel, M., Vanselow, M. and Trueper, H. G. |
| Title |
Siroheme sulfite reductase from Chromatium vinosum. Purification and investigation of some of its molecular and catalytic properties. |
| Journal |
Arch. Microbiol. 121 (1979) 29-36. |
| Reference |
|
| Authors |
Seki Y, Sogawa N, Ishimoto M |
| Title |
Siroheme as an active catalyst in sulfite reduction. |
| Journal |
J. Biochem. 90 (1981) 1487-92. |
| Reference |
|
| Authors |
Pott AS, Dahl C. |
| Title |
Sirohaem sulfite reductase and other proteins encoded by genes at the dsr locus of Chromatium vinosum are involved in the oxidation of intracellular sulfur. |
| Journal |
Microbiology. 144 ( Pt 7) (1998) 1881-94. |
| Sequence |
|
| Reference |
|
| Authors |
Oliveira TF, Vonrhein C, Matias PM, Venceslau SS, Pereira IA, Archer M |
| Title |
The crystal structure of Desulfovibrio vulgaris dissimilatory sulfite reductase bound to DsrC provides novel insights into the mechanism of sulfate respiration. |
| Journal |
J. Biol. Chem. 283 (2008) 34141-9. |
| Reference |
|
| Authors |
Venceslau SS, Stockdreher Y, Dahl C, Pereira IA |
| Title |
The "bacterial heterodisulfide" DsrC is a key protein in dissimilatory sulfur metabolism. |
| Journal |
Biochim. Biophys. Acta. 1837 (2014) 1148-64. |
| Other DBs |
ExplorEnz - The Enzyme Database: IUBMB Enzyme Nomenclature: ExPASy - ENZYME nomenclature database: BRENDA, the Enzyme Database: CAS: 37256-51-2 |