5M4X
Mutant glyceraldehyde dehydrogenase (F34M+Y399C+S405N) from Thermoplasma acidophilum
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004777 | molecular_function | succinate-semialdehyde dehydrogenase (NAD+) activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0006096 | biological_process | glycolytic process |
| A | 0009255 | biological_process | Entner-Doudoroff pathway through 6-phosphogluconate |
| A | 0009450 | biological_process | gamma-aminobutyric acid catabolic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0043796 | molecular_function | glyceraldehyde dehydrogenase (NADP+) activity |
| A | 0051289 | biological_process | protein homotetramerization |
| B | 0004777 | molecular_function | succinate-semialdehyde dehydrogenase (NAD+) activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0006096 | biological_process | glycolytic process |
| B | 0009255 | biological_process | Entner-Doudoroff pathway through 6-phosphogluconate |
| B | 0009450 | biological_process | gamma-aminobutyric acid catabolic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0043796 | molecular_function | glyceraldehyde dehydrogenase (NADP+) activity |
| B | 0051289 | biological_process | protein homotetramerization |
| C | 0004777 | molecular_function | succinate-semialdehyde dehydrogenase (NAD+) activity |
| C | 0005829 | cellular_component | cytosol |
| C | 0006096 | biological_process | glycolytic process |
| C | 0009255 | biological_process | Entner-Doudoroff pathway through 6-phosphogluconate |
| C | 0009450 | biological_process | gamma-aminobutyric acid catabolic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| C | 0042803 | molecular_function | protein homodimerization activity |
| C | 0043796 | molecular_function | glyceraldehyde dehydrogenase (NADP+) activity |
| C | 0051289 | biological_process | protein homotetramerization |
| D | 0004777 | molecular_function | succinate-semialdehyde dehydrogenase (NAD+) activity |
| D | 0005829 | cellular_component | cytosol |
| D | 0006096 | biological_process | glycolytic process |
| D | 0009255 | biological_process | Entner-Doudoroff pathway through 6-phosphogluconate |
| D | 0009450 | biological_process | gamma-aminobutyric acid catabolic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| D | 0042803 | molecular_function | protein homodimerization activity |
| D | 0043796 | molecular_function | glyceraldehyde dehydrogenase (NADP+) activity |
| D | 0051289 | biological_process | protein homotetramerization |
Functional Information from PROSITE/UniProt
| site_id | PS00070 |
| Number of Residues | 12 |
| Details | ALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. YwNAGQSCIAAE |
| Chain | Residue | Details |
| A | TYR274-GLU285 |
| site_id | PS00687 |
| Number of Residues | 8 |
| Details | ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. LELGGKAP |
| Chain | Residue | Details |
| A | LEU246-PRO253 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 88 |
| Details | Coiled coil: {"evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10007","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"P28037","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P28037","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"O57693","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q59931","evidenceCode":"ECO:0000250"},{"source":"UniProtKB","id":"Q84DC3","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 24 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q84DC3","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 92 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q59931","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P28037","evidenceCode":"ECO:0000250"},{"source":"UniProtKB","id":"Q59931","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 4 |
| Details | Site: {"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
