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IPR006067 is a Nitrite/sulphite reductase 4Fe-4S domain.
<p>Sulphite reductases (SiRs) and related nitrite reductases (NiRs) catalyse the six-electron reduction reactions of sulphite to sulphide, and nitrite to ammonia, respectively. The Escherichia coli SiR enzyme is a complex composed of two proteins, a flavoprotein alpha-component (SiR-FP) and a hemoprotein beta-component (SiR-HP) ([interpro:IPR005117]), and has an α(8)β(4) quaternary structure [[cite:PUB00014351]]. SiR-FP contains both FAD and FMN, while SiR-HP contains a Fe(4)S(4) cluster coupled to a siroheme through a cysteine bridge. Electrons are transferred from NADPH to FAD, and on to FMN in SiR-FP, from which they are transferred to the metal centre of SiR-HP, where they reduce the siroheme-bound sulphite.</p> <p>SiR-HP has a two-fold symmetry, which generates a distinctive three-domain α/β fold that controls assembly and reactivity [[cite:PUB00014496]]. In the E. coli SiR-HP enzyme ([ec:1.8.1.2]), the iron is bound to cysteine residues at positions 433, 439, 478 and 482, the latter also forming the siroheme ligand.</p>
This description is obtained from EB-eye REST.
GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on , while the GO metadata was last updated on .
| GO term | Namespace | Name | Definition | Relationships |
|---|---|---|---|---|
| Molecular function | Oxidoreductase activity | Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced. | ||
| Molecular function | Heme binding | Interacting selectively and non-covalently with heme, any compound of iron complexed in a porphyrin (tetrapyrrole) ring. | ||
| Molecular function | Iron-sulfur cluster binding | Interacting selectively and non-covalently with an iron-sulfur cluster, a combination of iron and sulfur atoms. | ||
| Biological process | Oxidation-reduction process | A metabolic process that results in the removal or addition of one or more electrons to or from a substance, with or without the concomitant removal or addition of a proton or protons. |
| Transcript | Name | Description | Predicted domains | Domain count |
|---|---|---|---|---|
| – | PREDICTED: sulfite reductase [ferredoxin] gi|356538473|ref|XP_003537728.1| | 15 | ||
| – | Ferredoxin-nitrite reductase [Lotus japonicus] gi|9968473|emb|CAC06095.1| | 14 | ||
| – | Ferredoxin-nitrite reductase [Lotus japonicus] gi|9968473|emb|CAC06095.1| | 13 | ||
| – | Ferredoxin-nitrite reductase [Lotus japonicus] gi|9968473|emb|CAC06095.1| | 13 | ||
| – | Sulfite reductase [NADPH] hemoprotein beta-component; TAIR: AT5G04590.1 sulfite reductase; Swiss-Prot: sp|Q75NZ0|SIR_PEA Sulfite reductase [ferredoxin], chloroplastic; TrEMBL-Plants: tr|A0A0B2P8I5|A0A0B2P8I5_GLYSO Sulfite reductase [ferredoxin]; Found in the gene: LotjaGi3g1v0537300 | 16 | ||
| – | Sulfite reductase [NADPH] hemoprotein beta-component; TAIR: AT5G04590.1 sulfite reductase; Swiss-Prot: sp|Q75NZ0|SIR_PEA Sulfite reductase [ferredoxin], chloroplastic; TrEMBL-Plants: tr|A0A0B2P8I5|A0A0B2P8I5_GLYSO Sulfite reductase [ferredoxin]; Found in the gene: LotjaGi3g1v0537300 | 17 | ||
| – | Nitrite reductase; TAIR: AT2G15620.1 nitrite reductase 1; Swiss-Prot: sp|P38500|NIR_BETPN Ferredoxin--nitrite reductase, chloroplastic; TrEMBL-Plants: tr|Q9FY16|Q9FY16_LOTJA Ferredoxin-nitrite reductase; Found in the gene: LotjaGi4g1v0074400 | 15 |
A list of co-occurring predicted domains within the L. japonicus gene space:
| Predicted domain | Source | Observations | Saturation (%) |
|---|---|---|---|
| SignalP-TM | SignalP_GRAM_NEGATIVE | 1 | 14.29 |