4R7T
Crystal structure of glucosamine-6-phosphate deaminase from Vibrio cholerae
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004342 | molecular_function | glucosamine-6-phosphate deaminase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0006043 | biological_process | glucosamine catabolic process |
| A | 0006044 | biological_process | N-acetylglucosamine metabolic process |
| A | 0006046 | biological_process | N-acetylglucosamine catabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0019262 | biological_process | N-acetylneuraminate catabolic process |
| A | 0042802 | molecular_function | identical protein binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004342 | molecular_function | glucosamine-6-phosphate deaminase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0006043 | biological_process | glucosamine catabolic process |
| B | 0006044 | biological_process | N-acetylglucosamine metabolic process |
| B | 0006046 | biological_process | N-acetylglucosamine catabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0019262 | biological_process | N-acetylneuraminate catabolic process |
| B | 0042802 | molecular_function | identical protein binding |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0004342 | molecular_function | glucosamine-6-phosphate deaminase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0005975 | biological_process | carbohydrate metabolic process |
| C | 0006043 | biological_process | glucosamine catabolic process |
| C | 0006044 | biological_process | N-acetylglucosamine metabolic process |
| C | 0006046 | biological_process | N-acetylglucosamine catabolic process |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0019262 | biological_process | N-acetylneuraminate catabolic process |
| C | 0042802 | molecular_function | identical protein binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 301 |
| Chain | Residue |
| A | ILE97 |
| A | HOH414 |
| A | HOH434 |
| A | HOH435 |
| B | ASP112 |
| site_id | AC2 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL A 302 |
| Chain | Residue |
| A | ASN140 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 303 |
| Chain | Residue |
| C | PRO149 |
| A | TYR254 |
| A | HOH427 |
| C | ASP141 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 300 |
| Chain | Residue |
| B | ILE97 |
| B | HOH422 |
| B | HOH435 |
| B | HOH451 |
| B | HOH452 |
| C | ASP112 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE FMT B 301 |
| Chain | Residue |
| B | GLY43 |
| B | THR44 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG C 300 |
| Chain | Residue |
| A | ASP112 |
| A | HOH420 |
| C | ILE97 |
| C | HOH434 |
| C | HOH463 |
| C | HOH464 |
Functional Information from PROSITE/UniProt
| site_id | PS01161 |
| Number of Residues | 19 |
| Details | GLC_GALNAC_ISOMERASE Glucosamine/galactosamine-6-phosphate isomerases signature. IksyGkInLfMgGVGnDGH |
| Chain | Residue | Details |
| A | ILE125-HIS143 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | Active site: {"description":"Proton acceptor; for enolization step","evidences":[{"source":"HAMAP-Rule","id":"MF_01241","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Active site: {"description":"For ring-opening step","evidences":[{"source":"HAMAP-Rule","id":"MF_01241","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | Active site: {"description":"Proton acceptor; for ring-opening step","evidences":[{"source":"HAMAP-Rule","id":"MF_01241","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 15 |
| Details | Site: {"description":"Part of the allosteric site","evidences":[{"source":"HAMAP-Rule","id":"MF_01241","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
