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UniProt functional annotation for P0AB87 | ||
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| UniProt code: P0AB87. |
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| Organism: | |
Escherichia coli (strain K12). |
| Taxonomy: | |
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia. |
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| Function: | |
Involved in the degradation of L-fucose and D-arabinose (PubMed:13898172). Catalyzes the reversible cleavage of L-fuculose 1- phosphate (Fuc1P) to yield dihydroxyacetone phosphate (DHAP) and L- lactaldehyde (PubMed:13898172, Ref.8, Ref.9, PubMed:10821675, PubMed:11054289). Also able to catalyze the reversible cleavage of D- ribulose 1-phosphate, but FucA has a higher affinity for L-fuculose 1- phosphate and L-lactaldehyde than for D-ribulose 1-phosphate and glycolaldehyde, respectively (PubMed:4928018). FucA possesses a high specificity for the dihydroxyacetone phosphate (DHAP), but accepts a great variety of different aldehydes and has a strong preference for L- configurated alpha-hydroxy aldehydes (PubMed:13898172, Ref.8, PubMed:10821675). FucA generates a vicinal diol unit having the absolute (3R,4R)-cis configuration (D-erythro) (Ref.8, PubMed:10821675). {ECO:0000269|PubMed:10821675, ECO:0000269|PubMed:11054289, ECO:0000269|PubMed:13898172, ECO:0000269|PubMed:4928018, ECO:0000269|Ref.8, ECO:0000269|Ref.9}. |
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| Catalytic activity: | |
Reaction=L-fuculose 1-phosphate = (S)-lactaldehyde + dihydroxyacetone phosphate; Xref=Rhea:RHEA:12933, ChEBI:CHEBI:18041, ChEBI:CHEBI:57642, ChEBI:CHEBI:57846; EC=4.1.2.17; Evidence={ECO:0000255|HAMAP-Rule:MF_00987, ECO:0000269|PubMed:10821675, ECO:0000269|PubMed:11054289, ECO:0000269|PubMed:13898172, ECO:0000269|Ref.8, ECO:0000269|Ref.9}; |
| Cofactor: | |
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_00987, ECO:0000269|PubMed:10821675, ECO:0000269|PubMed:11054289, ECO:0000269|PubMed:13898172, ECO:0000269|PubMed:15299567, ECO:0000269|PubMed:8515438, ECO:0000269|PubMed:8676381}; Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00987, ECO:0000269|PubMed:10821675, ECO:0000269|PubMed:11054289, ECO:0000269|PubMed:15299567, ECO:0000269|PubMed:8515438, ECO:0000269|PubMed:8676381}; |
| Activity regulation: | |
Inhibited by phosphoglycolohydroxamate (PGH). {ECO:0000269|Ref.9}. |
| Biophysicochemical properties: | |
Kinetic parameters: KM=0.7 mM for L-fuculose 1-phosphate (Fuc1P) {ECO:0000269|PubMed:13898172}; KM=1.5 mM for L-fuculose 1-phosphate (Fuc1P) {ECO:0000269|Ref.9}; KM=2.2 mM for L-fuculose 1-phosphate (Fuc1P) {ECO:0000269|PubMed:10821675}; Note=Kcat is 19.3 sec(-1) for L-fuculose 1-phosphate (Fuc1P) as substrate. {ECO:0000269|PubMed:10821675}; pH dependence: Optimum pH is 7.2. {ECO:0000269|PubMed:13898172}; |
| Pathway: | |
Carbohydrate degradation; L-fucose degradation; L-lactaldehyde and glycerone phosphate from L-fucose: step 3/3. {ECO:0000255|HAMAP- Rule:MF_00987, ECO:0000269|PubMed:13898172}. |
| Subunit: | |
Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00987, ECO:0000269|PubMed:10821675, ECO:0000269|PubMed:11054289, ECO:0000269|PubMed:15299567, ECO:0000269|PubMed:8515438, ECO:0000269|PubMed:8676381}. |
| Induction: | |
By L-fucose. {ECO:0000269|PubMed:4928018}. |
| Miscellaneous: | |
During catalysis the binding of dihydroxyacetone phosphate (DHAP) frees Glu-73 residue from its interaction with zinc ion (PubMed:10821675, PubMed:11054289). Then Glu-73 residue abstracts a proton from the C3 atom of dihydroxyacetone phosphate (DHAP) (or from the O4 atom of L-fuculose 1-phosphate (Fuc1P) in the backward reaction), and moves to transfer its proton to the aldehyde oxygen atom (or to the C3 atom of dihydroxyacetone phosphate (DHAP)) (PubMed:10821675, PubMed:11054289). {ECO:0000269|PubMed:10821675, ECO:0000269|PubMed:11054289}. |
| Similarity: | |
Belongs to the aldolase class II family. AraD/FucA subfamily. {ECO:0000255|HAMAP-Rule:MF_00987, ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.