1E47
L-Fuculose 1-Phosphate Aldolase from Escherichia coli Mutant E73Q
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| P | 0005829 | cellular_component | cytosol |
| P | 0005996 | biological_process | monosaccharide metabolic process |
| P | 0006004 | biological_process | fucose metabolic process |
| P | 0008270 | molecular_function | zinc ion binding |
| P | 0008738 | molecular_function | L-fuculose-phosphate aldolase activity |
| P | 0016829 | molecular_function | lyase activity |
| P | 0016830 | molecular_function | carbon-carbon lyase activity |
| P | 0016832 | molecular_function | aldehyde-lyase activity |
| P | 0019317 | biological_process | fucose catabolic process |
| P | 0019323 | biological_process | pentose catabolic process |
| P | 0019568 | biological_process | arabinose catabolic process |
| P | 0019571 | biological_process | D-arabinose catabolic process |
| P | 0042355 | biological_process | L-fucose catabolic process |
| P | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 P 301 |
| Chain | Residue |
| P | ASN29 |
| P | THR43 |
| P | SER71 |
| P | SER72 |
| P | 13P304 |
| P | HOH415 |
| P | HOH432 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 P 302 |
| Chain | Residue |
| P | TRP74 |
| P | ARG75 |
| P | HOH444 |
| P | HOH449 |
| P | HOH451 |
| P | HIS64 |
| P | GLY67 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue BME P 303 |
| Chain | Residue |
| P | CYS14 |
| P | GLY28 |
| P | HOH410 |
| P | HOH415 |
| site_id | AC4 |
| Number of Residues | 15 |
| Details | binding site for residue 13P P 304 |
| Chain | Residue |
| P | ALA27 |
| P | ASN29 |
| P | THR43 |
| P | SER71 |
| P | SER72 |
| P | GLN73 |
| P | HIS92 |
| P | HIS94 |
| P | TYR113 |
| P | HIS155 |
| P | SO4301 |
| P | ZN305 |
| P | HOH401 |
| P | HOH415 |
| P | HOH432 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue ZN P 305 |
| Chain | Residue |
| P | HIS92 |
| P | HIS94 |
| P | TYR113 |
| P | HIS155 |
| P | 13P304 |
| P | HOH401 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:10821675, ECO:0000269|PubMed:11054289 |
| Chain | Residue | Details |
| P | GLN73 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11054289, ECO:0000269|PubMed:8676381, ECO:0007744|PDB:1E47, ECO:0007744|PDB:1E48, ECO:0007744|PDB:4FUA |
| Chain | Residue | Details |
| P | GLY28 | |
| P | THR43 | |
| P | SER71 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00987, ECO:0000269|PubMed:10821675, ECO:0000269|PubMed:11054289, ECO:0000269|PubMed:15299567, ECO:0000269|PubMed:8676381, ECO:0007744|PDB:1DZU, ECO:0007744|PDB:1DZV, ECO:0007744|PDB:1DZW, ECO:0007744|PDB:1DZX, ECO:0007744|PDB:1DZY, ECO:0007744|PDB:1DZZ, ECO:0007744|PDB:1E48, ECO:0007744|PDB:1E49, ECO:0007744|PDB:1E4A, ECO:0007744|PDB:1E4B, ECO:0007744|PDB:1E4C, ECO:0007744|PDB:1FUA, ECO:0007744|PDB:2FUA, ECO:0007744|PDB:3FUA, ECO:0007744|PDB:4FUA |
| Chain | Residue | Details |
| P | GLN73 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00987, ECO:0000269|PubMed:10821675, ECO:0000269|PubMed:11054289, ECO:0000269|PubMed:15299567, ECO:0000269|PubMed:8676381, ECO:0007744|PDB:1DZU, ECO:0007744|PDB:1DZV, ECO:0007744|PDB:1DZW, ECO:0007744|PDB:1DZX, ECO:0007744|PDB:1DZY, ECO:0007744|PDB:1DZZ, ECO:0007744|PDB:1E46, ECO:0007744|PDB:1E47, ECO:0007744|PDB:1E48, ECO:0007744|PDB:1E49, ECO:0007744|PDB:1E4A, ECO:0007744|PDB:1E4B, ECO:0007744|PDB:1E4C, ECO:0007744|PDB:1FUA, ECO:0007744|PDB:2FUA, ECO:0007744|PDB:3FUA, ECO:0007744|PDB:4FUA |
| Chain | Residue | Details |
| P | HIS92 | |
| P | HIS94 | |
| P | HIS155 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | SITE: Plays a key role in the stabilization of the transition state and positioning the aldehyde component => ECO:0000269|PubMed:10821675 |
| Chain | Residue | Details |
| P | TYR113 | |
| P | PHE131 | |
| P | TYR209 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1fua |
| Chain | Residue | Details |
| P | TYR113 | |
| P | GLN73 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1fua |
| Chain | Residue | Details |
| P | ALA117 |
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 72 |
| Chain | Residue | Details |
| P | GLN73 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| P | HIS92 | metal ligand |
| P | HIS94 | metal ligand |
| P | TYR113 | electrostatic stabiliser, transition state stabiliser |
| P | HIS155 | metal ligand |
| P | TYR209 | electrostatic stabiliser, transition state stabiliser |
