9C91
Assimilatory NADPH-dependent sulfite reductase minimal dimer
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000103 | biological_process | sulfate assimilation |
| A | 0004783 | molecular_function | sulfite reductase (NADPH) activity |
| A | 0010181 | molecular_function | FMN binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0019344 | biological_process | L-cysteine biosynthetic process |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0000103 | biological_process | sulfate assimilation |
| B | 0004783 | molecular_function | sulfite reductase (NADPH) activity |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0009337 | cellular_component | sulfite reductase complex (NADPH) |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0019344 | biological_process | L-cysteine biosynthetic process |
| B | 0020037 | molecular_function | heme binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0050661 | molecular_function | NADP binding |
| B | 0051536 | molecular_function | iron-sulfur cluster binding |
| B | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| B | 0070814 | biological_process | hydrogen sulfide biosynthetic process |
Functional Information from PROSITE/UniProt
| site_id | PS00365 |
| Number of Residues | 17 |
| Details | NIR_SIR Nitrite and sulfite reductases iron-sulfur/siroheme-binding site. TGCpngCgramlaEVGL |
| Chain | Residue | Details |
| B | THR477-LEU493 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 138 |
| Details | Domain: {"description":"Flavodoxin-like","evidences":[{"source":"HAMAP-Rule","id":"MF_01541","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 214 |
| Details | Domain: {"description":"FAD-binding FR-type","evidences":[{"source":"HAMAP-Rule","id":"MF_01541","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 17 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01541","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15966732","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 18 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01541","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10860732","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"7569952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9315848","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"7569952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9315848","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 8 |
| Details | M-CSA 398 |
| Chain | Residue | Details |
| B | ARG83 | activator |
| B | ARG153 | activator |
| B | LYS215 | activator |
| B | LYS217 | activator |
| B | CYS434 | metal ligand |
| B | CYS440 | metal ligand |
| B | CYS479 | metal ligand |
| B | CYS483 | electron shuttle, metal ligand |
