| EC Tree |
| 1. Oxidoreductases |
| 1.8 Acting on a sulfur group of donors |
| 1.8.1 With NAD+ or NADP+ as acceptor |
| ID: | 1.8.1.2 | ||
|---|---|---|---|
| Description: | Assimilatory sulfite reductase (NADPH). | ||
| Alternative Name: |
Sulfite reductase (NADPH). | ||
| Prosite: | PDOC00314; | ||
| PDB: |
|
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| Cath: | 1.10.10.370; 1.10.287.3170; 3.30.1420.10; 3.30.413.10; 3.30.70.20; 3.30.70.250; 3.30.70.2500; 3.30.70.3340; 3.40.50.80; 3.90.480.10; |
Click one PDB to see exact 3D structure provided by NGL.
Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.| UniProtKB Enzyme Link: | UniProtKB 1.8.1.2 |
| BRENDA Enzyme Link: | BRENDA 1.8.1.2 |
| KEGG Enzyme Link: | KEGG1.8.1.2 |
| BioCyc Enzyme Link: | BioCyc 1.8.1.2 |
| ExPASy Enzyme Link: | ExPASy1.8.1.2 |
| EC2PDB Enzyme Link: | EC2PDB 1.8.1.2 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.8.1.2 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.8.1.2 |
| IntEnz Enzyme Link: | IntEnz 1.8.1.2 |
| MEDLINE Enzyme Link: | MEDLINE 1.8.1.2 |
| RHEA:13801 | 3 H2O + hydrogen sulfide + 3 NADP(+) = 4 H(+) + 3 NADPH + sulfite |
| RULE(radius=1) | [*:1]-[c;H0;+0:2]1:[cH;+0:3]:[cH;+0:4]:[cH;+0:5]:[n+;H0:6](-[*:7]):[cH;+0:8]:1.[*:9]-[n+;H0:10]1:[cH;+0:11]:[cH;+0:12]:[cH;+0:13]:[c;H0;+0:14](-[*:15]):[cH;+0:16]:1.[*:17]-[n+;H0:18]1:[cH;+0:19]:[cH;+0:20]:[cH;+0:21]:[c;H0;+0:22](-[*:23]):[cH;+0:24]:1.[OH2;+0:25].[OH2;+0:26].[OH2;+0:27].[SH2;+0:28]>>[*:1]-[C;H0;+0:2]1=[CH;+0:8]-[N;H0;+0:6](-[*:7])-[CH;+0:5]=[CH;+0:4]-[CH2;+0:3]-1.[*:9]-[N;H0;+0:10]1-[CH;+0:11]=[CH;+0:12]-[CH2;+0:13]-[C;H0;+0:14](-[*:15])=[CH;+0:16]-1.[*:17]-[N;H0;+0:18]1-[CH;+0:19]=[CH;+0:20]-[CH2;+0:21]-[C;H0;+0:22](-[*:23])=[CH;+0:24]-1.[O;H0;+0:27]=[S;H0;+0:28](-[OH;+0:25])-[OH;+0:26] |
| Reaction | ![]() |
| Core-to-Core |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Structures of the siroheme- and Fe4S4-containing active center of sulfite reductase in different states of oxidation: heme activation via reduction-gated exogenous ligand exchange. | Crane BR, Siegel LM, Getzoff ED | 1997 Oct 7 | 9315848 |
| Flavin mononucleotide-binding domain of the flavoprotein component of the sulfite reductase from Escherichia coli. | Coves J, Zeghouf M, Macherel D, Guigliarelli B, Asso M, Fontecave M | 1997 May 13 | 9153434 |
| Sequence analysis and expression of the Salmonella typhimurium asr operon encoding production of hydrogen sulfide from sulfite. | Huang CJ, Barrett EL | 1991 Feb | 1704886 |
| Four crystal structures of the 60 kDa flavoprotein monomer of the sulfite reductase indicate a disordered flavodoxin-like module. | Gruez A, Pignol D, Zeghouf M, Covès J, Fontecave M, Ferrer JL, Fontecilla-Camps JC | 2000 May 26 | 10860732 |