5WP0
Crystal structure of NAD synthetase NadE from Vibrio fischeri
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003952 | molecular_function | NAD+ synthase (glutamine-hydrolyzing) activity |
| A | 0004359 | molecular_function | glutaminase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0008795 | molecular_function | NAD+ synthase activity |
| A | 0009435 | biological_process | NAD biosynthetic process |
| A | 0016874 | molecular_function | ligase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0003952 | molecular_function | NAD+ synthase (glutamine-hydrolyzing) activity |
| B | 0004359 | molecular_function | glutaminase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0008795 | molecular_function | NAD+ synthase activity |
| B | 0009435 | biological_process | NAD biosynthetic process |
| B | 0016874 | molecular_function | ligase activity |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 20 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00193 |
| Chain | Residue | Details |
| A | GLY43 | |
| A | HIS266 | |
| B | GLY43 | |
| B | ASP49 | |
| B | ARG146 | |
| B | THR166 | |
| B | GLU171 | |
| B | LYS179 | |
| B | ASP186 | |
| B | LYS195 | |
| B | THR217 | |
| A | ASP49 | |
| B | HIS266 | |
| A | ARG146 | |
| A | THR166 | |
| A | GLU171 | |
| A | LYS179 | |
| A | ASP186 | |
| A | LYS195 | |
| A | THR217 |
