AC MF_01952; DC Protein; auto TR HAMAP; MF_01952; -; 1; level=0 XX Names: UlaF XX ID ULAF case DE RecName: Full=L-ribulose-5-phosphate 4-epimerase UlaF; DE EC=5.1.3.4; DE AltName: Full=L-ascorbate utilization protein F; DE AltName: Full=Phosphoribulose isomerase; end case case not DE RecName: Full=Putative L-ribulose-5-phosphate 4-epimerase; end case GN Name=ulaF; XX CC -!- FUNCTION: Catalyzes the isomerization of L-ribulose 5-phosphate to D- CC xylulose 5-phosphate. Is involved in the anaerobic L-ascorbate CC utilization. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-ribulose 5-phosphate = D-xylulose 5-phosphate; CC Xref=Rhea:RHEA:22368, ChEBI:CHEBI:57737, ChEBI:CHEBI:58226; CC EC=5.1.3.4; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Note=Binds 1 zinc ion per subunit.; CC -!- PATHWAY: Cofactor degradation; L-ascorbate degradation; D-xylulose 5- CC phosphate from L-ascorbate: step 4/4. CC -!- INDUCTION: Induced by L-ascorbate. Repressed by UlaR. CC -!- SIMILARITY: Belongs to the aldolase class II family. AraD/FucA CC subfamily. XX DR Pfam; PF00596; Aldolase_II; 1; trigger=no XX KW Carbohydrate metabolism KW Isomerase KW Metal-binding KW Zinc XX GO GO:0019852; P:L-ascorbic acid metabolic process GO GO:0008742; F:L-ribulose-phosphate 4-epimerase activity GO GO:0008270; F:zinc ion binding XX FT From: ULAF_ECOLI (P39306) FT BINDING 26..27 FT /ligand="substrate" FT Condition: G-N FT BINDING 43..44 FT /ligand="substrate" FT Condition: [TS]-G FT BINDING 72..73 FT /ligand="substrate" FT Condition: S-S FT ACT_SITE 118 FT /note="Proton donor/acceptor" FT Condition: D FT ACT_SITE 225 FT /note="Proton donor/acceptor" FT Condition: Y FT BINDING 74 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: D FT BINDING 93 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: H FT BINDING 95 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: H FT BINDING 167 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: H XX Size: 228-228; Related: None; Template: P39306; Scope: Bacteria; Enterobacteriaceae Fusion: Nter: None Cter: None Duplicate: None Plasmid: None Comments: None XX # Revision 1.23 2022/11/19 //