ID FUCA_ECO57 Reviewed; 215 AA. AC Q8X6R8; Q7AB69; DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2002, sequence version 1. DT 27-MAR-2024, entry version 121. 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}; GN OrderedLocusNames=Z4117, ECs3660; OS Escherichia coli O157:H7. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83334; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC; RX PubMed=11206551; DOI=10.1038/35054089; RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J., RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., RA Blattner F.R.; RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7."; RL Nature 409:529-533(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC; RX PubMed=11258796; DOI=10.1093/dnares/8.1.11; RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S., RA Shiba T., Hattori M., Shinagawa H.; RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and RT genomic comparison with a laboratory strain K-12."; RL DNA Res. 8:11-22(2001). 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; AE005174; AAG57914.1; -; Genomic_DNA. DR EMBL; BA000007; BAB37083.1; -; Genomic_DNA. DR PIR; D91086; D91086. DR PIR; F85931; F85931. DR RefSeq; NP_311687.1; NC_002695.1. DR RefSeq; WP_000440775.1; NZ_VOAI01000003.1. DR AlphaFoldDB; Q8X6R8; -. DR SMR; Q8X6R8; -. DR STRING; 155864.Z4117; -. DR GeneID; 75203809; -. DR GeneID; 916460; -. DR KEGG; ece:Z4117; -. DR KEGG; ecs:ECs_3660; -. DR PATRIC; fig|386585.9.peg.3826; -. DR eggNOG; COG0235; Bacteria. DR HOGENOM; CLU_006033_3_0_6; -. DR OMA; YATFGTH; -. DR UniPathway; UPA00563; UER00626. DR Proteomes; UP000000558; Chromosome. DR Proteomes; UP000002519; 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_0000162926" 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; 23785 MW; 072E4EC5A94E76D1 CRC64; MERNKLARQI IDTCLEMTRL GLNQGTAGNV SVRYQDGMLI TPTGIPYEKL TESHIVFIDG NGKHEEGKLP SSEWRFHMAA YQSRPDANAV VHNHAVHCTA VSILNRPIPA IHYMIAAAGG NSIPCAPYAT FGTRELSEHV ALALKNRKAT LLQHHGLIAC EVNLEKALWL AHEVEVLAQL YLTTLAITDP VPVLSDEEIA VVLEKFKTYG LRIEE //