Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0009234 | biological_process | menaquinone biosynthetic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0016854 | molecular_function | racemase and epimerase activity |
| A | 0043748 | molecular_function | O-succinylbenzoate synthase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0009234 | biological_process | menaquinone biosynthetic process |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0016854 | molecular_function | racemase and epimerase activity |
| B | 0043748 | molecular_function | O-succinylbenzoate synthase activity |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0009234 | biological_process | menaquinone biosynthetic process |
| C | 0016829 | molecular_function | lyase activity |
| C | 0016853 | molecular_function | isomerase activity |
| C | 0016854 | molecular_function | racemase and epimerase activity |
| C | 0043748 | molecular_function | O-succinylbenzoate synthase activity |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0009234 | biological_process | menaquinone biosynthetic process |
| D | 0016829 | molecular_function | lyase activity |
| D | 0016853 | molecular_function | isomerase activity |
| D | 0016854 | molecular_function | racemase and epimerase activity |
| D | 0043748 | molecular_function | O-succinylbenzoate synthase activity |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"15313614","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"15313614","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15313614","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1XPY","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15313614","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1XPY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1XS2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2GGH","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15313614","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1r6w |
| Chain | Residue | Details |
| A | LYS269 | |
| A | LYS168 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1r6w |
| Chain | Residue | Details |
| B | LYS269 | |
| B | LYS168 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1r6w |
| Chain | Residue | Details |
| C | LYS269 | |
| C | LYS168 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1r6w |
| Chain | Residue | Details |
| D | LYS269 | |
| D | LYS168 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1r6w |
| Chain | Residue | Details |
| A | LYS170 | |
| A | LYS269 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1r6w |
| Chain | Residue | Details |
| B | LYS170 | |
| B | LYS269 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1r6w |
| Chain | Residue | Details |
| C | LYS170 | |
| C | LYS269 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1r6w |
| Chain | Residue | Details |
| D | LYS170 | |
| D | LYS269 |
| site_id | MCSA1 |
| Number of Residues | 8 |
| Details | M-CSA 377 |
| Chain | Residue | Details |
| A | SER142 | transition state stabiliser |
| A | LYS168 | transition state stabiliser |
| A | LYS170 | proton donor |
| A | ASP195 | metal ligand |
| A | GLU220 | metal ligand |
| A | ASP245 | metal ligand |
| A | LYS269 | proton acceptor |
| A | GLY297 | transition state stabiliser |
| site_id | MCSA2 |
| Number of Residues | 8 |
| Details | M-CSA 377 |
| Chain | Residue | Details |
| B | SER142 | transition state stabiliser |
| B | LYS168 | transition state stabiliser |
| B | LYS170 | proton donor |
| B | ASP195 | metal ligand |
| B | GLU220 | metal ligand |
| B | ASP245 | metal ligand |
| B | LYS269 | proton acceptor |
| B | GLY297 | transition state stabiliser |
| site_id | MCSA3 |
| Number of Residues | 8 |
| Details | M-CSA 377 |
| Chain | Residue | Details |
| C | SER142 | transition state stabiliser |
| C | LYS168 | transition state stabiliser |
| C | LYS170 | proton donor |
| C | ASP195 | metal ligand |
| C | GLU220 | metal ligand |
| C | ASP245 | metal ligand |
| C | LYS269 | proton acceptor |
| C | GLY297 | transition state stabiliser |
| site_id | MCSA4 |
| Number of Residues | 8 |
| Details | M-CSA 377 |
| Chain | Residue | Details |
| D | SER142 | transition state stabiliser |
| D | LYS168 | transition state stabiliser |
| D | LYS170 | proton donor |
| D | ASP195 | metal ligand |
| D | GLU220 | metal ligand |
| D | ASP245 | metal ligand |
| D | LYS269 | proton acceptor |
| D | GLY297 | transition state stabiliser |
