ID ALF_HAEIN Reviewed; 359 AA. AC P44429; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 27-MAR-2024, entry version 127. DE RecName: Full=Fructose-bisphosphate aldolase; DE Short=FBP aldolase; DE Short=FBPA; DE EC=4.1.2.13; DE AltName: Full=Fructose-1,6-bisphosphate aldolase; GN Name=fba; OrderedLocusNames=HI_0524; 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: Catalyzes the aldol condensation of dihydroxyacetone CC phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate CC (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and CC the reverse reaction in glycolysis. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3- CC phosphate + dihydroxyacetone phosphate; Xref=Rhea:RHEA:14729, CC ChEBI:CHEBI:32966, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=4.1.2.13; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 2 Zn(2+) ions per subunit. One is catalytic and the other CC provides a structural contribution. {ECO:0000250}; CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- CC phosphate and glycerone phosphate from D-glucose: step 4/4. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the class II fructose-bisphosphate aldolase CC family. {ECO:0000305}. 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; AAC22182.1; -; Genomic_DNA. DR PIR; C64074; C64074. DR RefSeq; NP_438682.1; NC_000907.1. DR AlphaFoldDB; P44429; -. DR SMR; P44429; -. DR STRING; 71421.HI_0524; -. DR EnsemblBacteria; AAC22182; AAC22182; HI_0524. DR KEGG; hin:HI_0524; -. DR PATRIC; fig|71421.8.peg.543; -. DR eggNOG; COG0191; Bacteria. DR HOGENOM; CLU_036923_0_0_6; -. DR OrthoDB; 9803995at2; -. DR PhylomeDB; P44429; -. DR BioCyc; HINF71421:G1GJ1-537-MONOMER; -. DR UniPathway; UPA00109; UER00183. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IBA:GO_Central. DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central. DR GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central. DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central. DR CDD; cd00946; FBP_aldolase_IIA; 1. DR Gene3D; 3.20.20.70; Aldolase class I; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000771; FBA_II. DR InterPro; IPR006411; Fruct_bisP_bact. DR NCBIfam; TIGR00167; cbbA; 1. DR NCBIfam; TIGR01520; FruBisAldo_II_A; 1. DR PANTHER; PTHR30559:SF0; FRUCTOSE-BISPHOSPHATE ALDOLASE; 1. DR PANTHER; PTHR30559; FRUCTOSE-BISPHOSPHATE ALDOLASE CLASS 2; 1. DR Pfam; PF01116; F_bP_aldolase; 1. DR PIRSF; PIRSF001359; F_bP_aldolase_II; 1. DR SUPFAM; SSF51569; Aldolase; 1. DR PROSITE; PS00602; ALDOLASE_CLASS_II_1; 1. DR PROSITE; PS00806; ALDOLASE_CLASS_II_2; 1. PE 3: Inferred from homology; KW Glycolysis; Lyase; Metal-binding; Reference proteome; Zinc. FT CHAIN 1..359 FT /note="Fructose-bisphosphate aldolase" FT /id="PRO_0000178716" FT ACT_SITE 110 FT /note="Proton donor" FT /evidence="ECO:0000250" FT BINDING 62 FT /ligand="D-glyceraldehyde 3-phosphate" FT /ligand_id="ChEBI:CHEBI:59776" FT /evidence="ECO:0000250" FT BINDING 111 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 145 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 175 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 227 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 228 FT /ligand="dihydroxyacetone phosphate" FT /ligand_id="ChEBI:CHEBI:57642" FT /evidence="ECO:0000250" FT BINDING 265 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 266..268 FT /ligand="dihydroxyacetone phosphate" FT /ligand_id="ChEBI:CHEBI:57642" FT /evidence="ECO:0000250" FT BINDING 287..290 FT /ligand="dihydroxyacetone phosphate" FT /ligand_id="ChEBI:CHEBI:57642" FT /evidence="ECO:0000250" SQ SEQUENCE 359 AA; 39340 MW; 1EDDFCDD0B69E32C CRC64; MAKLLDIVKP GVVTGEDVQK VFAYAKEHNF AIPAVNCVGS DSVNAVLETA ARVKAPVIIQ FSNGGAAFYA GKGIKPTSGT RPDVLGAIAG AKQVHTLAKE YGVPVILHTD HAAKKLLPWI DGLLDAGEKH FAETGRPLFS SHMIDLSEES MEENMAICRE YLARMDKMGM TLEIEIGITG GEEDGVDNSD VDESRLYTQP SDVLYVYDQL HPVSPNFTVA AAFGNVHGVY KPGNVKLKPS ILGESQEFVS KERNLPAKPI NFVFHGGSGS SREEIREAIG YGAIKMNIDT DTQWASWNGI LNFYKANEAY LQGQLGNPEG PDAPNKKYYD PRVWLRKMEE SMSKRLEQSF EDLNCVDVL //