ID ALF2_STAEQ Reviewed; 286 AA. AC Q5HM97; DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 15-FEB-2005, sequence version 1. DT 27-MAR-2024, entry version 97. 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; Synonyms=fbaA; OrderedLocusNames=SERP1732; OS Staphylococcus epidermidis (strain ATCC 35984 / RP62A). OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=176279; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35984 / RP62A; RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005; RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J., RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J., RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H., RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L., RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E., RA Fraser C.M.; RT "Insights on evolution of virulence and resistance from the complete genome RT analysis of an early methicillin-resistant Staphylococcus aureus strain and RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis RT strain."; RL J. Bacteriol. 187:2426-2438(2005). 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; CP000029; AAW55054.1; -; Genomic_DNA. DR RefSeq; WP_001829938.1; NC_002976.3. DR AlphaFoldDB; Q5HM97; -. DR SMR; Q5HM97; -. DR STRING; 176279.SERP1732; -. DR GeneID; 50018178; -. DR KEGG; ser:SERP1732; -. DR eggNOG; COG0191; Bacteria. DR HOGENOM; CLU_040088_0_1_9; -. DR UniPathway; UPA00109; UER00183. DR Proteomes; UP000000531; 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; PS00806; ALDOLASE_CLASS_II_2; 1. PE 3: Inferred from homology; KW Glycolysis; Lyase; Metal-binding; Reference proteome; Zinc. FT CHAIN 1..286 FT /note="Fructose-bisphosphate aldolase" FT /id="PRO_0000178742" 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 107 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 137 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 181 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 182 FT /ligand="dihydroxyacetone phosphate" FT /ligand_id="ChEBI:CHEBI:57642" FT /evidence="ECO:0000250" FT BINDING 209 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 210..212 FT /ligand="dihydroxyacetone phosphate" FT /ligand_id="ChEBI:CHEBI:57642" FT /evidence="ECO:0000250" FT BINDING 231..234 FT /ligand="dihydroxyacetone phosphate" FT /ligand_id="ChEBI:CHEBI:57642" FT /evidence="ECO:0000250" SQ SEQUENCE 286 AA; 30883 MW; D11CBF24BAE3B4E6 CRC64; MPLVSMKEML IDAKENGYAV GQYNLNNLEF TQAILEASQE ENAPVILGVS EGAARYMSGF YTVVKMVEGL MHDLNITIPV AIHLDHGSSF EKCKEAIDAG FTSVMIDASH SPFEENVEIT SKVVEYAHDR GVSVEAELGT VGGQEDDVVA DGVIYADPKE CQELVEKTGI DTLAPALGSV HGPYKGEPKL GFKEMEEIGA STGLPLVLHG GTGIPTKDIQ KAIPYGTAKI NVNTENQIAS AKAVREVLNN DKDVYDPRKY LGPAREAIKE TVKGKIREFG TSNRAK //