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UniProt functional annotation for P32719 | ||
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| UniProt code: P32719. |
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| Organism: | |
Escherichia coli (strain K12). |
| Taxonomy: | |
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia. |
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| Function: | |
Catalyzes the reversible epimerization of D-allulose 6- phosphate to D-fructose 6-phosphate. Can also catalyze with lower efficiency the reversible epimerization of D-ribulose 5-phosphate to D- xylulose 5-phosphate. {ECO:0000255|HAMAP-Rule:MF_02226, ECO:0000269|PubMed:18700786, ECO:0000269|PubMed:9401019}. |
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| Catalytic activity: | |
Reaction=D-allulose 6-phosphate = keto-D-fructose 6-phosphate; Xref=Rhea:RHEA:28426, ChEBI:CHEBI:57579, ChEBI:CHEBI:61519; Evidence={ECO:0000255|HAMAP-Rule:MF_02226, ECO:0000269|PubMed:18700786}; |
| Cofactor: | |
Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000269|PubMed:18700786}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:18700786}; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:18700786}; Note=Binds 1 divalent metal cation per subunit. Activity is highest with Co(2+) > Mn(2+) > Zn(2+). {ECO:0000269|PubMed:18700786}; |
| Pathway: | |
Carbohydrate degradation; D-allose degradation. {ECO:0000255|HAMAP-Rule:MF_02226, ECO:0000269|PubMed:18700786}. |
| Subunit: | |
Homohexamer. Trimer of dimers. {ECO:0000269|PubMed:18700786}. |
| Similarity: | |
Belongs to the ribulose-phosphate 3-epimerase family. AlsE subfamily. {ECO:0000255|HAMAP-Rule:MF_02226, ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.