8J5D
Cryo-EM structure of starch degradation complex of BAM1-LSF1-MDH
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000272 | biological_process | polysaccharide catabolic process |
| A | 0016161 | molecular_function | beta-amylase activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0006099 | biological_process | tricarboxylic acid cycle |
| B | 0006108 | biological_process | malate metabolic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016615 | molecular_function | malate dehydrogenase activity |
| B | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| B | 0019752 | biological_process | carboxylic acid metabolic process |
| B | 0030060 | molecular_function | L-malate dehydrogenase (NAD+) activity |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0006099 | biological_process | tricarboxylic acid cycle |
| C | 0006108 | biological_process | malate metabolic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016615 | molecular_function | malate dehydrogenase activity |
| C | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| C | 0019752 | biological_process | carboxylic acid metabolic process |
| C | 0030060 | molecular_function | L-malate dehydrogenase (NAD+) activity |
| D | 0006470 | biological_process | protein dephosphorylation |
| D | 0016311 | biological_process | dephosphorylation |
| D | 0019203 | molecular_function | carbohydrate phosphatase activity |
Functional Information from PROSITE/UniProt
| site_id | PS00068 |
| Number of Residues | 13 |
| Details | MDH Malate dehydrogenase active site signature. VTTLDvvRAntfV |
| Chain | Residue | Details |
| B | VAL227-VAL239 |
| site_id | PS00506 |
| Number of Residues | 9 |
| Details | BETA_AMYLASE_1 Beta-amylase active site 1. HqCGGNVGD |
| Chain | Residue | Details |
| A | HIS187-ASP195 |
| site_id | PS00679 |
| Number of Residues | 11 |
| Details | BETA_AMYLASE_2 Beta-amylase active site 2. GpAGELRYPSY |
| Chain | Residue | Details |
| A | GLY275-TYR285 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10050","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10050","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"P11708","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 22 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P40926","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P11708","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
