ID ALF_STRP8 Reviewed; 293 AA. AC P68906; P82486; DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 90. 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=spyM18_1954; OS Streptococcus pyogenes serotype M18 (strain MGAS8232). OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=186103; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGAS8232; RX PubMed=11917108; DOI=10.1073/pnas.062526099; RA Smoot J.C., Barbian K.D., Van Gompel J.J., Smoot L.M., Chaussee M.S., RA Sylva G.L., Sturdevant D.E., Ricklefs S.M., Porcella S.F., Parkins L.D., RA Beres S.B., Campbell D.S., Smith T.M., Zhang Q., Kapur V., Daly J.A., RA Veasy L.G., Musser J.M.; RT "Genome sequence and comparative microarray analysis of serotype M18 group RT A Streptococcus strains associated with acute rheumatic fever outbreaks."; RL Proc. Natl. Acad. Sci. U.S.A. 99:4668-4673(2002). 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 -!- 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; AE009949; AAL98448.1; -; Genomic_DNA. DR RefSeq; WP_002982850.1; NC_003485.1. DR AlphaFoldDB; P68906; -. DR SMR; P68906; -. DR KEGG; spm:spyM18_1954; -. DR HOGENOM; CLU_040088_0_1_9; -. DR UniPathway; UPA00109; UER00183. DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:UniProtKB-EC. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IEA:InterPro. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway. DR CDD; cd00947; TBP_aldolase_IIB; 1. DR Gene3D; 3.20.20.70; Aldolase class I; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000771; FBA_II. DR InterPro; IPR011289; Fruc_bis_ald_class-2. DR NCBIfam; TIGR00167; cbbA; 1. DR NCBIfam; TIGR01859; fruc_bis_ald; 1. DR PANTHER; PTHR30304; D-TAGATOSE-1,6-BISPHOSPHATE ALDOLASE; 1. DR PANTHER; PTHR30304:SF0; D-TAGATOSE-1,6-BISPHOSPHATE ALDOLASE SUBUNIT GATY-RELATED; 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; Zinc. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250" FT CHAIN 2..293 FT /note="Fructose-bisphosphate aldolase" FT /id="PRO_0000178750" FT ACT_SITE 85 FT /note="Proton donor" FT /evidence="ECO:0000250" FT BINDING 50 FT /ligand="D-glyceraldehyde 3-phosphate" FT /ligand_id="ChEBI:CHEBI:59776" FT /evidence="ECO:0000250" FT BINDING 86 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 106 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 136 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 178 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 179 FT /ligand="dihydroxyacetone phosphate" FT /ligand_id="ChEBI:CHEBI:57642" FT /evidence="ECO:0000250" FT BINDING 208 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 209..211 FT /ligand="dihydroxyacetone phosphate" FT /ligand_id="ChEBI:CHEBI:57642" FT /evidence="ECO:0000250" FT BINDING 230..233 FT /ligand="dihydroxyacetone phosphate" FT /ligand_id="ChEBI:CHEBI:57642" FT /evidence="ECO:0000250" SQ SEQUENCE 293 AA; 31208 MW; 8ECD3C3E41A79FD2 CRC64; MAIVSAEKFV QAARENGYAV GGFNTNNLEW TQAILRAAEA KQAPVLIQTS MGAAKYMGGY KVCQSLITNL VESMGITVPV AIHLDHGHYE DALECIEVGY TSIMFDGSHL PVEENLAKTA EVVKIAHAKG VSVEAEVGTI GGEEDGIIGK GELAPIEDAK AMVETGIDFL AAGIGNIHGP YPENWEGLAL DHLEKLTAAV PGFPIVLHGG SGIPDDQIKE AIRLGVAKVN VNTESQIAFS NATREFARNY EANEAEYDGK KLFDPRKFLA PGMKAVQGAV EERIDVFGSA NKA //