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UniProt functional annotation for P39304 | ||
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| UniProt code: P39304. |
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| Organism: | |
Escherichia coli (strain K12). |
| Taxonomy: | |
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia. |
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| Function: | |
Catalyzes the decarboxylation of 3-keto-L-gulonate-6-P into L-xylulose-5-P. Is involved in the anaerobic L-ascorbate utilization. {ECO:0000269|PubMed:11741871}. |
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| Catalytic activity: | |
Reaction=3-dehydro-L-gulonate 6-phosphate + H(+) = CO2 + L-xylulose 5- phosphate; Xref=Rhea:RHEA:14353, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57829, ChEBI:CHEBI:58774; EC=4.1.1.85; |
| Cofactor: | |
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Note=Binds 1 Mg(2+) ion per subunit.; |
| Biophysicochemical properties: | |
Kinetic parameters: KM=0.67 mM for 3-keto-L-gulonate-6-P {ECO:0000269|PubMed:15157077}; |
| Pathway: | |
Cofactor degradation; L-ascorbate degradation; D-xylulose 5- phosphate from L-ascorbate: step 2/4. |
| Subunit: | |
Homodimer. {ECO:0000269|PubMed:11900527, ECO:0000269|PubMed:15157078, ECO:0000269|PubMed:15697207}. |
| Induction: | |
Induced by L-ascorbate. Repressed by UlaR. {ECO:0000269|PubMed:12374842, ECO:0000269|PubMed:14996803}. |
| Miscellaneous: | |
The reaction mechanism proceeds via the formation of a Mg(2+) ion-stabilized 1,2-cis-enediolate intermediate. Water molecules competitively shuttle protons from the side chains of His-136 and Arg- 139 to alternate faces of this intermediate. The active site is located at the interface of the component polypeptides. |
| Similarity: | |
Belongs to the HPS/KGPDC family. KGPDC subfamily. {ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.