ID ALF_STRP6 Reviewed; 293 AA. AC Q5XA12; P82486; DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 99. 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=M6_Spy1616; OS Streptococcus pyogenes serotype M6 (strain ATCC BAA-946 / MGAS10394). OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=286636; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-946 / MGAS10394; RX PubMed=15272401; DOI=10.1086/422697; RA Banks D.J., Porcella S.F., Barbian K.D., Beres S.B., Philips L.E., RA Voyich J.M., DeLeo F.R., Martin J.M., Somerville G.A., Musser J.M.; RT "Progress toward characterization of the group A Streptococcus metagenome: RT complete genome sequence of a macrolide-resistant serotype M6 strain."; RL J. Infect. Dis. 190:727-738(2004). RN [2] RP PROTEIN SEQUENCE OF 2-12; 15-36; 130-150; 196-219; 224-244 AND 284-293, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=JRS4 / Serotype M6; RA Hogan D.A., Du P., Stevenson T.I., Whitton M., Kilby G.W., Rogers J., RA VanBogelen R.A.; RT "Two-dimensional gel electrophoresis map of Streptococcus pyogenes RT proteins."; RL Submitted (MAY-2000) to UniProtKB. 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; CP000003; AAT87751.1; -; Genomic_DNA. DR RefSeq; WP_011184946.1; NC_006086.1. DR AlphaFoldDB; Q5XA12; -. DR SMR; Q5XA12; -. DR KEGG; spa:M6_Spy1616; -. DR HOGENOM; CLU_040088_0_1_9; -. DR UniPathway; UPA00109; UER00183. DR Proteomes; UP000001167; Chromosome. 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 1: Evidence at protein level; KW Direct protein sequencing; Glycolysis; Lyase; Metal-binding; Zinc. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|Ref.2" FT CHAIN 2..293 FT /note="Fructose-bisphosphate aldolase" FT /id="PRO_0000178749" 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; 31136 MW; 29B9DF899FCCA085 CRC64; MAIVSAEKFV QAARENGYAV GGFNTNNLEW TQAILRAAEA KQAPVLIQTS MGAAKYMGGY KVCQSLITNL VESMGITVPV AIHLDHGHYG DALECIEVGY TSIMFDGSHL PVEENLAKTA EVVKIAHAKG VSVEAEVGTI GGEEDGIIGK GELAPIEDAK AMVETGIDFL AAGIGNIHGP YPENWEGLAL DHLEKLTAAV PGFPIVLHGG SGIPDDQIKE AIRLGVAKVN VNTESQIAFS NATREFARNY EANEAEYDGK KLFDPRKFLA PGMKAVQGAV EERIDVFGSA NKA //