Literature summary for 5.1.3.22 extracted from

Shi, R.; Pineda, M.; Ajamian, E.; Cui, Q.; Matte, A.; Cygler, M.
Structure of L-xylulose-5-Phosphate 3-epimerase (UlaE) from the anaerobic L-ascorbate utilization pathway of Escherichia coli: identification of a novel phosphate binding motif within a TIM barrel fold (2008), J. Bacteriol., 190, 8137-8144.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
protein has a triosephosphate isomerase barrel fold and forms dimers. The active site is located at the C-terminal ends of the parallel beta-strands. The enzyme binds Zn2+, which is coordinated by Glu155, Asp185, His211, and Glu251. A phosphate-binding site is formed by residues from the beta1/alpha1 loop and alpha3'-helix in the N-terminal region	Escherichia coli

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Zn2+	the enzyme binds Zn2+, which is coordinated by Glu155, Asp185, His211, and Glu25, crystallization data	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Subunits

Subunits	Comment	Organism
dimer	crystallization data	Escherichia coli

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Release 2023.1 (January 2023)