7LQM
Glucosamie-6-phosphate Deaminase from Pasturella multocida
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004342 | molecular_function | glucosamine-6-phosphate deaminase activity |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0006044 | biological_process | N-acetylglucosamine metabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0019262 | biological_process | N-acetylneuraminate catabolic process |
| B | 0004342 | molecular_function | glucosamine-6-phosphate deaminase activity |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0006044 | biological_process | N-acetylglucosamine metabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0019262 | biological_process | N-acetylneuraminate catabolic process |
| C | 0004342 | molecular_function | glucosamine-6-phosphate deaminase activity |
| C | 0005975 | biological_process | carbohydrate metabolic process |
| C | 0006044 | biological_process | N-acetylglucosamine metabolic process |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0019262 | biological_process | N-acetylneuraminate catabolic process |
| D | 0004342 | molecular_function | glucosamine-6-phosphate deaminase activity |
| D | 0005975 | biological_process | carbohydrate metabolic process |
| D | 0006044 | biological_process | N-acetylglucosamine metabolic process |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0019262 | biological_process | N-acetylneuraminate catabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 301 |
| Chain | Residue |
| B | GLU138 |
| B | LYS139 |
| B | SER142 |
| B | HOH322 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue EDO C 301 |
| Chain | Residue |
| D | TYR100 |
| C | EDO303 |
| D | PRO55 |
| D | THR56 |
| D | MET86 |
| D | ASP87 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue EDO C 302 |
| Chain | Residue |
| D | GLN134 |
| D | GLU137 |
| D | ARG171 |
| D | THR172 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue EDO C 303 |
| Chain | Residue |
| C | EDO301 |
| D | THR56 |
| D | GLY152 |
| D | VAL153 |
| D | LYS223 |
Functional Information from PROSITE/UniProt
| site_id | PS01161 |
| Number of Residues | 19 |
| Details | GLC_GALNAC_ISOMERASE Glucosamine/galactosamine-6-phosphate isomerases signature. IksyGkIhLfMgGVGvDGH |
| Chain | Residue | Details |
| A | ILE140-HIS158 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor; for enolization step => ECO:0000255|HAMAP-Rule:MF_01241 |
| Chain | Residue | Details |
| A | ASP87 | |
| B | ASP87 | |
| C | ASP87 | |
| D | ASP87 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | ACT_SITE: For ring-opening step => ECO:0000255|HAMAP-Rule:MF_01241 |
| Chain | Residue | Details |
| A | ASP156 | |
| A | GLU163 | |
| B | ASP156 | |
| B | GLU163 | |
| C | ASP156 | |
| C | GLU163 | |
| D | ASP156 | |
| D | GLU163 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor; for ring-opening step => ECO:0000255|HAMAP-Rule:MF_01241 |
| Chain | Residue | Details |
| A | HIS158 | |
| B | HIS158 | |
| C | HIS158 | |
| D | HIS158 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 20 |
| Details | SITE: Part of the allosteric site => ECO:0000255|HAMAP-Rule:MF_01241 |
| Chain | Residue | Details |
| A | SER166 | |
| B | TYR269 | |
| C | SER166 | |
| C | ARG173 | |
| C | LYS175 | |
| C | THR176 | |
| C | TYR269 | |
| D | SER166 | |
| D | ARG173 | |
| D | LYS175 | |
| D | THR176 | |
| A | ARG173 | |
| D | TYR269 | |
| A | LYS175 | |
| A | THR176 | |
| A | TYR269 | |
| B | SER166 | |
| B | ARG173 | |
| B | LYS175 | |
| B | THR176 |
