5U0M
Fatty aldehyde dehydrogenase from Marinobacter aquaeolei VT8 and cofactor complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006525 | biological_process | arginine metabolic process |
| A | 0006527 | biological_process | L-arginine 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 | 0019544 | biological_process | L-arginine catabolic process to L-glutamate |
| A | 0019545 | biological_process | L-arginine catabolic process to succinate |
| A | 0043824 | molecular_function | succinylglutamate-semialdehyde dehydrogenase activity |
| B | 0006525 | biological_process | arginine metabolic process |
| B | 0006527 | biological_process | L-arginine 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 | 0019544 | biological_process | L-arginine catabolic process to L-glutamate |
| B | 0019545 | biological_process | L-arginine catabolic process to succinate |
| B | 0043824 | molecular_function | succinylglutamate-semialdehyde dehydrogenase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 501 |
| Chain | Residue |
| A | SER227 |
| A | THR228 |
| A | HIS231 |
| A | ARG404 |
| A | TYR405 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 502 |
| Chain | Residue |
| A | ARG66 |
| A | HIS137 |
| A | ARG138 |
| A | HOH606 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | binding site for residue CIT A 503 |
| Chain | Residue |
| A | PHE151 |
| A | HIS154 |
| A | LEU155 |
| A | ARG281 |
| A | CYS282 |
| A | THR283 |
| A | THR438 |
| A | GLY439 |
| A | ALA440 |
| A | PHE446 |
| site_id | AC4 |
| Number of Residues | 20 |
| Details | binding site for residue NAD A 504 |
| Chain | Residue |
| A | PHE146 |
| A | TYR149 |
| A | ASN150 |
| A | LEU155 |
| A | LYS173 |
| A | PRO174 |
| A | SER175 |
| A | GLU176 |
| A | GLY209 |
| A | THR224 |
| A | GLY225 |
| A | SER226 |
| A | VAL229 |
| A | GLU248 |
| A | MET249 |
| A | GLY250 |
| A | CYS282 |
| A | GLU379 |
| A | PHE381 |
| A | HOH607 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | binding site for residue EDO B 501 |
| Chain | Residue |
| B | PHE393 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | binding site for residue CIT B 502 |
| Chain | Residue |
| B | PHE151 |
| B | HIS154 |
| B | LEU155 |
| B | ARG281 |
| B | CYS282 |
| B | THR283 |
| B | THR438 |
| B | GLY439 |
| B | ALA440 |
| site_id | AC7 |
| Number of Residues | 21 |
| Details | binding site for residue NAD B 503 |
| Chain | Residue |
| B | PHE146 |
| B | GLY147 |
| B | PRO148 |
| B | TYR149 |
| B | ASN150 |
| B | LEU155 |
| B | LYS173 |
| B | PRO174 |
| B | SER175 |
| B | GLU176 |
| B | GLY209 |
| B | THR224 |
| B | GLY225 |
| B | SER226 |
| B | VAL229 |
| B | GLU248 |
| B | MET249 |
| B | CYS282 |
| B | GLU379 |
| B | PHE381 |
| B | PHE446 |
Functional Information from PROSITE/UniProt
| site_id | PS00070 |
| Number of Residues | 12 |
| Details | ALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. FlSAGQRCTCAR |
| Chain | Residue | Details |
| A | PHE275-ARG286 |
| site_id | PS00687 |
| Number of Residues | 8 |
| Details | ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. LEMGGNNP |
| Chain | Residue | Details |
| A | LEU247-PRO254 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01174","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01174","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
