| UniProt functional annotation for P05042 | |||
| UniProt code: P05042. |
| Organism: | Escherichia coli (strain K12). | |
| Taxonomy: | Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia. | |
| Function: | Involved in the TCA cycle. FumC seems to be a backup enzyme for FumA under conditions of iron limitation and oxidative stress (PubMed:7592392). Catalyzes the stereospecific interconversion of fumarate to L-malate (PubMed:1917897, PubMed:3282546). {ECO:0000269|PubMed:1917897, ECO:0000269|PubMed:3282546, ECO:0000269|PubMed:7592392, ECO:0000305|PubMed:8496960}. | |
| Catalytic activity: | Reaction=(S)-malate = fumarate + H2O; Xref=Rhea:RHEA:12460, ChEBI:CHEBI:15377, ChEBI:CHEBI:15589, ChEBI:CHEBI:29806; EC=4.2.1.2; Evidence={ECO:0000255|HAMAP-Rule:MF_00743, ECO:0000269|PubMed:1917897, ECO:0000269|PubMed:3282546}; | |
| Activity regulation: | Inhibited by ATP, citrate and S-2,3- dicarboxyaziridine. {ECO:0000269|PubMed:1917897}. | |
| Biophysicochemical properties: | Kinetic parameters: KM=50 uM for L-malate (at pH 7.3 and 30 degrees Celsius) {ECO:0000269|PubMed:1917897}; KM=207 uM for fumarate (at pH 7.9) {ECO:0000269|PubMed:12021453}; KM=390 uM for fumarate {ECO:0000269|PubMed:3282546}; KM=857 uM for S-malate (at pH 7.9) {ECO:0000269|PubMed:12021453}; KM=2.94 mM for S-malate {ECO:0000269|PubMed:3282546}; Vmax=1 umol/min/mg enzyme for fumarate {ECO:0000269|PubMed:3282546}; Vmax=1 umol/min/mg enzyme for S-malate {ECO:0000269|PubMed:3282546}; Vmax=344.8 umol/min/mg enzyme for fumarate (at pH 7.9) {ECO:0000269|PubMed:12021453}; Vmax=176.8 umol/min/mg enzyme for S-malate (at pH 7.9) {ECO:0000269|PubMed:12021453}; Note=Kcat is 1149 sec(-1) for fumarate (at pH 7.9). Kcat is 595.2 sec(-1) for S-malate (at pH 7.9). {ECO:0000269|PubMed:12021453}; pH dependence: Optimum pH is 8. {ECO:0000269|PubMed:1917897}; Temperature dependence: Thermostable. {ECO:0000269|PubMed:3282546}; | |
| Pathway: | Carbohydrate metabolism; tricarboxylic acid cycle; (S)-malate from fumarate: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00743, ECO:0000305}. | |
| Subunit: | Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00743, ECO:0000269|PubMed:12021453, ECO:0000269|PubMed:1917897, ECO:0000269|PubMed:3282546, ECO:0000269|PubMed:8496960, ECO:0000269|PubMed:8909293, ECO:0000269|PubMed:9098893}. | |
| Subcellular location: | Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00743, ECO:0000305}. | |
| Induction: | Under conditions of iron limitation and oxidative stress. {ECO:0000269|PubMed:3282546, ECO:0000269|PubMed:7592392}. | |
| Disruption phenotype: | Cells lacking this gene show an increase of biofilm formation. {ECO:0000269|PubMed:17222132}. | |
| Miscellaneous: | There are 2 substrate-binding sites: the catalytic A site, and the non-catalytic B site that may play a role in the transfer of substrate or product between the active site and the solvent. Alternatively, the B site may bind allosteric effectors. {ECO:0000255|HAMAP-Rule:MF_00743, ECO:0000305|PubMed:14990798, ECO:0000305|PubMed:9098893}. | |
| Similarity: | Belongs to the class-II fumarase/aspartase family. Fumarase subfamily. {ECO:0000255|HAMAP-Rule:MF_00743, ECO:0000305}. | |
Annotations taken from UniProtKB at the EBI.