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UniProt functional annotation for P08200 | ||
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| UniProt code: P08200. |
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| Organism: | |
Escherichia coli (strain K12). |
| Taxonomy: | |
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia. |
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| Catalytic activity: | |
Reaction=D-threo-isocitrate + NADP(+) = 2-oxoglutarate + CO2 + NADPH; Xref=Rhea:RHEA:19629, ChEBI:CHEBI:15562, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.42; Evidence={ECO:0000269|PubMed:21151122, ECO:0000269|PubMed:3112144, ECO:0000269|PubMed:7761851, ECO:0000269|PubMed:7819221}; |
| Cofactor: | |
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:7761851}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000269|PubMed:11284679, ECO:0000269|PubMed:7761851}; |
| Activity regulation: | |
Inhibition of this enzyme by phosphorylation regulates the branch point between the Krebs cycle and the glyoxylate bypass, which is an alternate route that accumulates carbon for biosynthesis when acetate is the sole carbon source for growth. {ECO:0000305|PubMed:3112144}. |
| Biophysicochemical properties: | |
Kinetic parameters: KM=11.4 uM for isocitrate {ECO:0000269|PubMed:7819221}; KM=13 uM for isocitrate {ECO:0000269|PubMed:7761851}; |
| Subunit: | |
Homodimer. {ECO:0000269|PubMed:11284679, ECO:0000269|PubMed:2204109, ECO:0000269|PubMed:2682654, ECO:0000269|PubMed:7761851}. |
| Ptm: | |
Phosphorylation state of this enzyme is controlled by isocitrate dehydrogenase kinase/phosphatase (AceK). {ECO:0000269|PubMed:2204109}. |
| Ptm: | |
Succinylation probably inhibits enzymatic activity. {ECO:0000269|PubMed:21151122}. |
| Similarity: | |
Belongs to the isocitrate and isopropylmalate dehydrogenases family. {ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.