Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0003824 | molecular_function | catalytic activity |
A | 0004474 | molecular_function | malate synthase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006097 | biological_process | glyoxylate cycle |
A | 0006099 | biological_process | tricarboxylic acid cycle |
A | 0009436 | biological_process | glyoxylate catabolic process |
A | 0016740 | molecular_function | transferase activity |
A | 0046872 | molecular_function | metal ion binding |
B | 0000287 | molecular_function | magnesium ion binding |
B | 0003824 | molecular_function | catalytic activity |
B | 0004474 | molecular_function | malate synthase activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0006097 | biological_process | glyoxylate cycle |
B | 0006099 | biological_process | tricarboxylic acid cycle |
B | 0009436 | biological_process | glyoxylate catabolic process |
B | 0016740 | molecular_function | transferase activity |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from PROSITE/UniProt
site_id | PS00589 |
Number of Residues | 16 |
Details | PTS_HPR_SER PTS HPR domain serine phosphorylation site signature. EIsLHgRSLLFIRnVG |
Chain | Residue | Details |
A | GLU326-GLY341 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor |
Chain | Residue | Details |
A | ARG338 | |
B | ARG338 | |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor |
Chain | Residue | Details |
A | ASP631 | |
B | ASP631 | |
site_id | SWS_FT_FI3 |
Number of Residues | 18 |
Details | BINDING: |
Chain | Residue | Details |
A | VAL118 | |
B | VAL118 | |
B | ARG125 | |
B | SER274 | |
B | ARG311 | |
B | ARG338 | |
B | GLU427 | |
B | GLY452 | |
B | ASP455 | |
B | PRO536 | |
A | ARG125 | |
A | SER274 | |
A | ARG311 | |
A | ARG338 | |
A | GLU427 | |
A | GLY452 | |
A | ASP455 | |
A | PRO536 | |
Chain | Residue | Details |
A | CYS617 | |
A | CYS688 | |
B | CYS617 | |
B | CYS688 | |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 6 |
Details | M-CSA 53 |
Chain | Residue | Details |
A | ASP270 | electrostatic stabiliser, hydrogen bond acceptor |
A | GLU272 | electrostatic stabiliser, hydrogen bond acceptor |
A | ARG338 | electrostatic stabiliser, hydrogen bond donor |
A | GLU427 | metal ligand |
A | ASP455 | metal ligand |
A | ASP631 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
site_id | MCSA2 |
Number of Residues | 6 |
Details | M-CSA 53 |
Chain | Residue | Details |
B | ASP270 | electrostatic stabiliser, hydrogen bond acceptor |
B | GLU272 | electrostatic stabiliser, hydrogen bond acceptor |
B | ARG338 | electrostatic stabiliser, hydrogen bond donor |
B | GLU427 | metal ligand |
B | ASP455 | metal ligand |
B | ASP631 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |