UniProt functional annotation for P32055

UniProt code: P32055.

Organism: Escherichia coli (strain K12).
Taxonomy: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia.
 
Function: Catalyzes the two-step NADP-dependent conversion of GDP-4- dehydro-6-deoxy-D-mannose to GDP-fucose, involving an epimerase and a reductase reaction. {ECO:0000255|HAMAP-Rule:MF_00956, ECO:0000269|PubMed:10480878, ECO:0000269|PubMed:11021971, ECO:0000269|PubMed:9473059}.
 
Catalytic activity: Reaction=GDP-beta-L-fucose + NADP(+) = GDP-4-dehydro-alpha-D-rhamnose + H(+) + NADPH; Xref=Rhea:RHEA:18885, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:57783, ChEBI:CHEBI:57964, ChEBI:CHEBI:58349; EC=1.1.1.271; Evidence={ECO:0000255|HAMAP- Rule:MF_00956, ECO:0000269|PubMed:10480878, ECO:0000269|PubMed:11021971, ECO:0000269|PubMed:9473059};
Activity regulation: Subject to product inhibition by NADP and GDP- fucose. {ECO:0000269|PubMed:10480878}.
Biophysicochemical properties: Kinetic parameters: KM=9 uM for NADPH {ECO:0000269|PubMed:10480878, ECO:0000269|PubMed:11021971}; KM=109 uM for NADH {ECO:0000269|PubMed:10480878, ECO:0000269|PubMed:11021971}; KM=29 uM for GDP-4-keto-6-deoxymannose {ECO:0000269|PubMed:10480878, ECO:0000269|PubMed:11021971}; Vmax=363.5 umol/min/mg enzyme {ECO:0000269|PubMed:10480878, ECO:0000269|PubMed:11021971}; pH dependence: Optimum pH is 6-6.5. {ECO:0000269|PubMed:10480878, ECO:0000269|PubMed:11021971};
Pathway: Nucleotide-sugar biosynthesis; GDP-L-fucose biosynthesis via de novo pathway; GDP-L-fucose from GDP-alpha-D-mannose: step 2/2. {ECO:0000255|HAMAP-Rule:MF_00956, ECO:0000269|PubMed:9473059}.
Pathway: Exopolysaccharide biosynthesis; colanic acid biosynthesis. {ECO:0000269|PubMed:9473059}.
Subunit: Homodimer. {ECO:0000269|PubMed:11021971, ECO:0000269|PubMed:9817848, ECO:0000269|PubMed:9862812}.
Subcellular location: Cytoplasm.
Similarity: Belongs to the NAD(P)-dependent epimerase/dehydratase family. Fucose synthase subfamily. {ECO:0000255|HAMAP-Rule:MF_00956}.

Annotations taken from UniProtKB at the EBI.