ID ALF_SINMW Reviewed; 359 AA. AC P56888; A6UGF3; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 13-NOV-2007, sequence version 2. DT 27-MAR-2024, entry version 114. 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=cbbA; OrderedLocusNames=Smed_3923; OS Sinorhizobium medicae (strain WSM419) (Ensifer medicae). OG Plasmid pSMED01. OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium. OX NCBI_TaxID=366394; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Fenner B.J., Tiwari R.P., Dilworth M.J.; RT "Genetic regulation of C1 metabolism in Sinorhizobium meliloti."; RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WSM419; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Reeve W.G., RA Richardson P.; RT "Complete sequence of Sinorhizobium medicae WSM419 plasmid pSMED01."; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. 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 biosynthesis; Calvin cycle. 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 -!- SEQUENCE CAUTION: CC Sequence=AAF25378.1; Type=Frameshift; Evidence={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; AF211846; AAF25378.1; ALT_FRAME; Genomic_DNA. DR EMBL; CP000739; ABR62733.1; -; Genomic_DNA. DR RefSeq; WP_011969555.1; NC_009620.1. DR RefSeq; YP_001312666.1; NC_009620.1. DR AlphaFoldDB; P56888; -. DR SMR; P56888; -. DR GeneID; 61612432; -. DR KEGG; smd:Smed_3923; -. DR PATRIC; fig|366394.8.peg.369; -. DR HOGENOM; CLU_040088_0_0_5; -. DR OrthoDB; 9803995at2; -. DR UniPathway; UPA00109; UER00183. DR UniPathway; UPA00116; -. DR Proteomes; UP000001108; Plasmid pSMED01. 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:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway. DR GO; GO:0019253; P:reductive pentose-phosphate cycle; 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; IPR006412; Fruct_bisP_Calv. DR NCBIfam; TIGR00167; cbbA; 1. DR NCBIfam; TIGR01521; FruBisAldo_II_B; 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 Calvin cycle; Glycolysis; Lyase; Metal-binding; Plasmid; Zinc. FT CHAIN 1..359 FT /note="Fructose-bisphosphate aldolase" FT /id="PRO_0000178730" FT ACT_SITE 83 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 84 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 105 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 142 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 198 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 199 FT /ligand="dihydroxyacetone phosphate" FT /ligand_id="ChEBI:CHEBI:57642" FT /evidence="ECO:0000250" FT BINDING 232 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 233..235 FT /ligand="dihydroxyacetone phosphate" FT /ligand_id="ChEBI:CHEBI:57642" FT /evidence="ECO:0000250" FT BINDING 275..278 FT /ligand="dihydroxyacetone phosphate" FT /ligand_id="ChEBI:CHEBI:57642" FT /evidence="ECO:0000250" FT CONFLICT 89..90 FT /note="AT -> PN (in Ref. 1; AAF25378)" FT /evidence="ECO:0000305" SQ SEQUENCE 359 AA; 38925 MW; 00D2342753333700 CRC64; MARITLRQLL DHAAERSYGV PAFNINNMEQ GLAIMEAARA CDAPVILQVS RGARSYANDI MLAKMMEALE VMYPDIPLCI HQDHGNNVAT CLTAIQHGFT SVMMDGSLKE DAKTPADYAY NAMITTEVSR LAHMVGASVE GELGCLGSLE TGHGEAEDGH GFEGALDRSQ LLTDPDEAAR FVAETGVDAL AVAIGTSHGA YKFTRKPTGE VLAMDVIEKI HERLPDTHIV MHGSSSVPQE WQDVFNAHGG EMRETYGVPV EEIVRGIRFG VRKVNIDTDL RLAAAAAFRR VADTSRTEFD PRKFLKPAMD AMSAVCKARF EAFGTAGNAS RIKVVPMAEM ARRYASGSLK PQAKRAEAA //