1EPS
STRUCTURE AND TOPOLOGICAL SYMMETRY OF THE GLYPHOSPHATE 5-ENOL-PYRUVYLSHIKIMATE-3-PHOSPHATE SYNTHASE: A DISTINCTIVE PROTEIN FOLD
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0003855 | molecular_function | 3-dehydroquinate dehydratase activity |
| A | 0003866 | molecular_function | 3-phosphoshikimate 1-carboxyvinyltransferase activity |
| A | 0004764 | molecular_function | shikimate 3-dehydrogenase (NADP+) activity |
| A | 0004765 | molecular_function | shikimate kinase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0009073 | biological_process | aromatic amino acid family biosynthetic process |
| A | 0009423 | biological_process | chorismate biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00210, ECO:0000269|PubMed:11171958, ECO:0000269|PubMed:12430021, ECO:0000269|PubMed:15736934, ECO:0000269|PubMed:16225867, ECO:0000269|PubMed:17855366, ECO:0000269|PubMed:17958399, ECO:0000269|PubMed:19211556 |
| Chain | Residue | Details |
| A | ASP313 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_00210, ECO:0000269|PubMed:15736934, ECO:0000305|PubMed:11171958 |
| Chain | Residue | Details |
| A | GLU341 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00210, ECO:0000269|PubMed:11171958, ECO:0000269|PubMed:12430021, ECO:0000269|PubMed:13129913, ECO:0000269|PubMed:15736934, ECO:0000269|PubMed:16225867, ECO:0000269|PubMed:17855366, ECO:0000269|PubMed:17958399, ECO:0000269|PubMed:19211556 |
| Chain | Residue | Details |
| A | LYS22 | |
| A | SER169 | |
| A | LYS340 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00210, ECO:0000269|PubMed:11171958, ECO:0000269|PubMed:12430021, ECO:0000269|PubMed:13129913, ECO:0000269|PubMed:15736934, ECO:0000269|PubMed:17855366, ECO:0000269|PubMed:17958399, ECO:0000269|PubMed:19211556 |
| Chain | Residue | Details |
| A | ARG27 | |
| A | SER197 | |
| A | ASN336 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00210, ECO:0000269|PubMed:11171958, ECO:0000269|PubMed:16225867, ECO:0000269|PubMed:17855366, ECO:0000269|PubMed:19211556 |
| Chain | Residue | Details |
| A | ARG124 | |
| A | ARG344 | |
| A | ARG386 | |
| A | LYS411 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | SITE: Modified by bromopyruvate => ECO:0000269|PubMed:11171958 |
| Chain | Residue | Details |
| A | CYS408 | |
| A | LYS411 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 7 |
| Details | M-CSA 457 |
| Chain | Residue | Details |
| A | ASP49 | metal ligand |
| A | ASN94 | metal ligand |
| A | ASP313 | electrostatic stabiliser, proton shuttle (general acid/base) |
| A | GLU341 | electrostatic stabiliser, metal ligand, proton shuttle (general acid/base) |
| A | HIS385 | steric role |
| A | ARG386 | transition state stabiliser |
| A | LYS411 | steric role |
