Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004333 | molecular_function | fumarate hydratase activity |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005759 | cellular_component | mitochondrial matrix |
| A | 0005829 | cellular_component | cytosol |
| A | 0006099 | biological_process | tricarboxylic acid cycle |
| A | 0006106 | biological_process | fumarate metabolic process |
| A | 0006108 | biological_process | malate metabolic process |
| A | 0006281 | biological_process | DNA repair |
| A | 0006302 | biological_process | double-strand break repair |
| A | 0006974 | biological_process | DNA damage response |
| A | 0016829 | molecular_function | lyase activity |
Functional Information from PDB Data
| site_id | AVE |
| Number of Residues | 1 |
| Details | AUTHOR STATED THIS AS MULTI-SUBUNIT ACTIVE SITE OF FUMARASE, WITH H213, T126, S124, AND N166 ALL PROVIDING HYDROGEN BONDS TO THE PUTATIVE CATALYTIC WATER MOLECULE. |
Functional Information from PROSITE/UniProt
| site_id | PS00163 |
| Number of Residues | 10 |
| Details | FUMARATE_LYASES Fumarate lyases signature. GSsiMpGKvN |
| Chain | Residue | Details |
| A | GLY342-ASN351 | |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | HIS213 | |
| Chain | Residue | Details |
| A | SER343 | |
| Chain | Residue | Details |
| A | SER124 | |
| A | SER164 | |
| Chain | Residue | Details |
| A | HIS154 | |
| Chain | Residue | Details |
| A | SER344 | |
| A | LYS349 | |
| A | THR212 | |
| Chain | Residue | Details |
| A | GLU356 | |
| Chain | Residue | Details |
| A | THR428 | |
