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 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 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 | ACT_SITE: Phosphocysteine intermediate => ECO:0000255|PROSITE-ProRule:PRU00160 |
Chain | Residue | Details |
D | CYS390 | |
C | HIS258 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
D | CYS390 | |
C | MET309 | |
B | ASP115 | |
B | ASN175 | |
B | ILE198 | |
B | MET309 | |
C | GLY89 | |
C | ASP115 | |
C | ASN175 | |
C | ILE198 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P11708 |
Chain | Residue | Details |
B | ARG162 | |
B | ARG168 | |
B | ASN200 | |
B | ARG234 | |
C | ARG162 | |
C | ARG168 | |
C | ASN200 | |
C | ARG234 |