ID FUCA_HAEIN Reviewed; 216 AA. AC P44777; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 27-MAR-2024, entry version 135. 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=HI_0611; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F., RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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; L42023; AAC22270.1; -; Genomic_DNA. DR PIR; C64081; C64081. DR RefSeq; NP_438769.1; NC_000907.1. DR AlphaFoldDB; P44777; -. DR SMR; P44777; -. DR STRING; 71421.HI_0611; -. DR EnsemblBacteria; AAC22270; AAC22270; HI_0611. DR KEGG; hin:HI_0611; -. DR PATRIC; fig|71421.8.peg.635; -. DR eggNOG; COG0235; Bacteria. DR HOGENOM; CLU_006033_3_0_6; -. DR OrthoDB; 5500703at2; -. DR PhylomeDB; P44777; -. DR BioCyc; HINF71421:G1GJ1-632-MONOMER; -. DR UniPathway; UPA00563; UER00626. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0016832; F:aldehyde-lyase activity; IBA:GO_Central. 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 GO; GO:0019323; P:pentose catabolic process; IBA:GO_Central. 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..216 FT /note="L-fuculose phosphate aldolase" FT /id="PRO_0000162928" 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 216 AA; 23944 MW; 4DBEEE21ED8EA6C6 CRC64; MNRAELSQKI IDTCLEMTKL GLNQGTAGNV SVRYKDGMLI TPTGMPYHLM KTENIVYVDG NGKHEENKLP SSEWQFHLSV YHTRPEANAV VHNHSIHCAG LSILEKPIPA IHYMVAVSGT DHIPCVPYAT FGSHKLASYV ATGIKESKAI LLAHHGLITC GENLDKALWL AQEVEVLASW YLKLLSTGLE IPLLSKEQMQ VVLGKFHTYG LRIEES //