ID FUCA_SHIFL Reviewed; 215 AA. AC P0AB88; P11550; DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 08-NOV-2005, sequence version 1. DT 27-MAR-2024, entry version 109. 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=SF2814, S3009; OS Shigella flexneri. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=623; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=301 / Serotype 2a; RX PubMed=12384590; DOI=10.1093/nar/gkf566; RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.; RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity RT through comparison with genomes of Escherichia coli K12 and O157."; RL Nucleic Acids Res. 30:4432-4441(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700930 / 2457T / Serotype 2a; RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003; RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G., RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T., RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.; RT "Complete genome sequence and comparative genomics of Shigella flexneri RT serotype 2a strain 2457T."; RL Infect. Immun. 71:2775-2786(2003). 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; AE005674; AAN44302.1; -; Genomic_DNA. DR EMBL; AE014073; AAP18127.1; -; Genomic_DNA. DR RefSeq; NP_708595.1; NC_004337.2. DR RefSeq; WP_000440781.1; NZ_WPGW01000008.1. DR AlphaFoldDB; P0AB88; -. DR SMR; P0AB88; -. DR STRING; 198214.SF2814; -. DR PaxDb; 198214-SF2814; -. DR GeneID; 1025774; -. DR GeneID; 75172884; -. DR KEGG; sfl:SF2814; -. DR KEGG; sfx:S3009; -. DR PATRIC; fig|198214.7.peg.3348; -. DR HOGENOM; CLU_006033_3_0_6; -. DR UniPathway; UPA00563; UER00626. DR Proteomes; UP000001006; Chromosome. DR Proteomes; UP000002673; 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_0000162929" 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; 23775 MW; BA9897E13ABE4A22 CRC64; MERNKLARQI IDTCLEMTRL GLNQGTAGNV SVRYQDGMLI TPTGIPYEKL TESHIVFIDG NGKHEEGKLP SSEWRFHMAA YQSRPDANAV VHNHAVHCTA VSILNRSIPA IHYMIAAAGG NSIPCAPYAT FGTRELSEHV ALALKNRKAT LLQHHGLIAC EVNLEKALWL AHEVEVLAQL YLTTLAITDP VPVLSDEEIA VVLEKFKTYG LRIEE //