Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004333 | molecular_function | fumarate hydratase activity |
| A | 0005515 | molecular_function | protein binding |
| 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
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"UniProtKB","id":"P05042","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"evidences":[{"source":"UniProtKB","id":"P9WN93","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P05042","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | Binding site: {"description":"in site B","evidences":[{"source":"UniProtKB","id":"P05042","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P9WN93","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Site: {"description":"Important for catalytic activity","evidences":[{"source":"UniProtKB","id":"P05042","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"17761666","evidenceCode":"ECO:0007744"}]} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1auw |
| Chain | Residue | Details |
| A | GLU356 | |
| A | SER343 | |
| A | LYS349 | |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1auw |
| Chain | Residue | Details |
| A | THR212 | |
| A | HIS213 | |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1auw |
| Chain | Residue | Details |
| A | GLU356 | |
| A | LYS349 | |
