5U0M
Fatty aldehyde dehydrogenase from Marinobacter aquaeolei VT8 and cofactor complex
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004029 | molecular_function | aldehyde dehydrogenase (NAD+) activity |
A | 0006525 | biological_process | arginine metabolic process |
A | 0006527 | biological_process | 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 | arginine catabolic process to glutamate |
A | 0019545 | biological_process | arginine catabolic process to succinate |
A | 0043824 | molecular_function | succinylglutamate-semialdehyde dehydrogenase activity |
B | 0004029 | molecular_function | aldehyde dehydrogenase (NAD+) activity |
B | 0006525 | biological_process | arginine metabolic process |
B | 0006527 | biological_process | 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 | arginine catabolic process to glutamate |
B | 0019545 | biological_process | 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 | ACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_01174 |
Chain | Residue | Details |
A | GLU248 | |
A | CYS282 | |
B | GLU248 | |
B | CYS282 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01174 |
Chain | Residue | Details |
A | GLY225 | |
B | GLY225 |