ID FUCA_ECOL6 Reviewed; 215 AA. AC Q8FEF0; DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 27-MAR-2024, entry version 103. DE RecName: Full=L-fuculose phosphate aldolase {ECO:0000255|HAMAP-Rule:MF_00987}; DE EC=4.1.2.17 {ECO:0000255|HAMAP-Rule:MF_00987}; DE AltName: Full=L-fuculose-1-phosphate aldolase {ECO:0000255|HAMAP-Rule:MF_00987}; GN Name=fucA {ECO:0000255|HAMAP-Rule:MF_00987}; OrderedLocusNames=c3368; OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=199310; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CFT073 / ATCC 700928 / UPEC; RX PubMed=12471157; DOI=10.1073/pnas.252529799; RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., RA Donnenberg M.S., Blattner F.R.; RT "Extensive mosaic structure revealed by the complete genome sequence of RT uropathogenic Escherichia coli."; RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002). CC -!- FUNCTION: Involved in the degradation of L-fucose and D-arabinose. CC Catalyzes the reversible cleavage of L-fuculose 1-phosphate (Fuc1P) to CC yield dihydroxyacetone phosphate (DHAP) and L-lactaldehyde. CC {ECO:0000255|HAMAP-Rule:MF_00987}. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-fuculose 1-phosphate = (S)-lactaldehyde + dihydroxyacetone CC phosphate; Xref=Rhea:RHEA:12933, ChEBI:CHEBI:18041, CC ChEBI:CHEBI:57642, ChEBI:CHEBI:57846; EC=4.1.2.17; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00987}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00987}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00987}; CC -!- PATHWAY: Carbohydrate degradation; L-fucose degradation; L-lactaldehyde CC and glycerone phosphate from L-fucose: step 3/3. {ECO:0000255|HAMAP- CC Rule:MF_00987}. CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00987}. CC -!- SIMILARITY: Belongs to the aldolase class II family. AraD/FucA CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00987}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE014075; AAN81815.1; -; Genomic_DNA. DR RefSeq; WP_000440772.1; NZ_CP051263.1. DR AlphaFoldDB; Q8FEF0; -. DR SMR; Q8FEF0; -. DR STRING; 199310.c3368; -. DR KEGG; ecc:c3368; -. DR eggNOG; COG0235; Bacteria. DR HOGENOM; CLU_006033_3_0_6; -. DR BioCyc; ECOL199310:C3368-MONOMER; -. DR UniPathway; UPA00563; UER00626. DR Proteomes; UP000001410; Chromosome. DR GO; GO:0008738; F:L-fuculose-phosphate aldolase activity; IEA:UniProtKB-UniRule. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0019568; P:arabinose catabolic process; IEA:UniProtKB-KW. DR GO; GO:0042355; P:L-fucose catabolic process; IEA:UniProtKB-UniRule. DR CDD; cd00398; Aldolase_II; 1. DR Gene3D; 3.40.225.10; Class II aldolase/adducin N-terminal domain; 1. DR HAMAP; MF_00987; FucA; 1. DR InterPro; IPR001303; Aldolase_II/adducin_N. DR InterPro; IPR036409; Aldolase_II/adducin_N_sf. DR InterPro; IPR004782; FucA. DR NCBIfam; TIGR01086; fucA; 1. DR PANTHER; PTHR22789:SF0; 3-OXO-TETRONATE 4-PHOSPHATE DECARBOXYLASE-RELATED; 1. DR PANTHER; PTHR22789; FUCULOSE PHOSPHATE ALDOLASE; 1. DR Pfam; PF00596; Aldolase_II; 1. DR SMART; SM01007; Aldolase_II; 1. DR SUPFAM; SSF53639; AraD/HMP-PK domain-like; 1. PE 3: Inferred from homology; KW Arabinose catabolism; Carbohydrate metabolism; Fucose metabolism; Lyase; KW Metal-binding; Reference proteome; Zinc. FT CHAIN 1..215 FT /note="L-fuculose phosphate aldolase" FT /id="PRO_0000162927" FT ACT_SITE 73 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00987" FT BINDING 28..29 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00987" FT BINDING 43..44 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00987" FT BINDING 71..72 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00987" FT BINDING 73 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00987" FT BINDING 92 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00987" FT BINDING 94 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00987" FT BINDING 155 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00987" FT SITE 113 FT /note="Plays a key role in the stabilization of the FT transition state and positioning the aldehyde component" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00987" FT SITE 131 FT /note="Plays a key role in the stabilization of the FT transition state and positioning the aldehyde component" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00987" FT SITE 209 FT /note="Plays a key role in the stabilization of the FT transition state and positioning the aldehyde component" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00987" SQ SEQUENCE 215 AA; 23757 MW; B0394EC5A9574B67 CRC64; MERNKLARQI IDTCLEMTRL GLNQGTAGNV SVRYQDGMLI TPTGIPYEKL TESHIVFIDG NGKHEEGKLP SSEWRFHMAA YQSRPDANAV VHNHAVHCTA VSILNRPIPA IHYMIAAAGG NSIPCAPYAT FGTRELSEHV ALALKNRKAT LLQHHGLIAC EANLEKALWL AHEVEVLAQL YLTTLAITDP VPVLSDEEIA VVLEKFKTYG LRIEE //