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InterPro: IPR011806 Sulphite reductase, dissimilatory-type alpha subunit

Protein matchesHelp
UniProtKB
Matches:
1349 proteins
AccessionHelp IPR011806 DsrA
TypeHelp Family
SignaturesHelp
InterPro RelationshipsHelp
Contains IPR006067 Nitrite/sulphite reductase 4Fe-4S domain
IPR017896 4Fe-4S ferredoxin, iron-sulpur binding domain
GO Term annotationHelp
Process GO:0055114 oxidation reduction
Function GO:0018551 hydrogensulfite reductase activity
GO:0020037 heme binding
GO:0051539 4 iron, 4 sulfur cluster binding
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

Dissimilatory sulphite reductase catalyzes the six-electron reduction of sulphite to sulphide, as the terminal reaction in dissimilatory sulphate reduction. It remains unclear however, whether trithionate and thiosulphate serve as intermediate compounds to sulphide, or as end products of sulphite reduction [1]. Sulphite reductase is a multisubunit enzyme composed of dimers of either alpha/beta or alpha/beta/gamma subunits, each containing a siroheme and iron sulphur cluster prosthetic centre [2]. Found in sulphate-reducing bacteria, these genes are commonly located in a unidirectional gene cluster [3].

Structural linksHelp
Database linksHelp
Enzyme: EC:1.8.99.3
PRIAM: PRI002226

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR011806 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
P45574 Sulfite reductase, dissimilatory-type subunit alpha

Q59109 Sulfite reductase, dissimilatory-type subunit alpha

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR006067 Nitrite/sulphite reductase 4Fe-4S domain
IPR011806 Sulphite reductase, dissimilatory-type alpha subunit
IPR017896 4Fe-4S ferredoxin, iron-sulpur binding domain
IPR005117 Nitrite/sulphite reductase, hemoprotein beta-component, ferrodoxin-like
PDB Chain
ModBase
SCOP Domain

PublicationsHelp
1. Hansen TA.
Metabolism of sulfate-reducing prokaryotes.
Antonie Van Leeuwenhoek 66 165-85 1994 [PubMed: 7747930]
http://dx.doi.org/10.1007/BF00871638
2. Pierik AJ, Duyvis MG, van Helvoort JM, Wolbert RB, Hagen WR.
The third subunit of desulfoviridin-type dissimilatory sulfite reductases.
Eur. J. Biochem. 205 111-5 1992 [PubMed: 1555572]
http://dx.doi.org/10.1111/j.1432-1033.1992.tb16757.x
3. Larsen O , Lien T, Birkeland NK.
A novel organization of the dissimilatory sulfite reductase operon of Thermodesulforhabdus norvegica verified by RT-PCR.
FEMS Microbiol. Lett. 203 81-5 2001 [PubMed: 11557144]
http://dx.doi.org/10.1111/j.1574-6968.2001.tb10824.x

Additional ReadingHelp
Schiffer A, Parey K, Warkentin E, Diederichs K, Huber H, Stetter KO, Kroneck PM, Ermler U.
Structure of the dissimilatory sulfite reductase from the hyperthermophilic archaeon Archaeoglobus fulgidus.
J. Mol. Biol. 379 2008 1063-74 [PubMed: 18495156]
http://dx.doi.org/10.1016/j.jmb.2008.04.027
Oliveira TF, Vonrhein C, Matias PM, Venceslau SS, Pereira IA, Archer M.
Purification, crystallization and preliminary crystallographic analysis of a dissimilatory sulfite reductase DsrAB in complex with DsrC.
J. Struct. Biol. 2008 [PubMed: 18706503]
Oliveira TF, Vonrhein C, Matias PM, Venceslau SS, Pereira IA, Archer M.
The crystal structure of Desulfovibrio vulgaris dissimilatory sulfite reductase bound to DsrC provides novel insights into the mechanism of sulfate respiration.
J. Biol. Chem. 283 2008 34141-9 [PubMed: 18829451]
http://dx.doi.org/10.1074/jbc.M805643200
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InterPro 24.0