ID ALF2_CERSP Reviewed; 354 AA. AC P29271; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-1992, sequence version 1. DT 13-SEP-2023, entry version 93. DE RecName: Full=Fructose-bisphosphate aldolase 2; DE Short=FBP aldolase; DE Short=FBPA; DE EC=4.1.2.13; DE AltName: Full=Fructose-1,6-bisphosphate aldolase; DE AltName: Full=Fructose-bisphosphate aldolase II; GN Name=cfxB; OS Cereibacter sphaeroides (Rhodobacter sphaeroides). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales; OC Paracoccaceae; Cereibacter. OX NCBI_TaxID=1063; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1939098; DOI=10.1016/s0021-9258(18)54944-9; RA Chen J.-H., Gibson J.L., McCue L.A., Tabita F.R.; RT "Identification, expression, and deduced primary structure of transketolase RT and other enzymes encoded within the form II CO2 fixation operon of RT Rhodobacter sphaeroides."; RL J. Biol. Chem. 266:20447-20452(1991). 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. CC -!- MISCELLANEOUS: This protein is encoded within the form II ribulose- CC bisphosphate carboxylase operon. 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; M68914; AAA26157.1; -; Genomic_DNA. DR PIR; D41080; D41080. DR RefSeq; WP_011339169.1; NZ_WSNV01000001.1. DR AlphaFoldDB; P29271; -. DR SMR; P29271; -. DR UniPathway; UPA00109; UER00183. DR UniPathway; UPA00116; -. 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; Zinc. FT CHAIN 1..354 FT /note="Fructose-bisphosphate aldolase 2" FT /id="PRO_0000178733" 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" SQ SEQUENCE 354 AA; 38269 MW; 9F547E84FC72ACF5 CRC64; MALITLRQLL DHAAEQGYGV PAFNINNMEQ GLAIMEAARA CDAPVIIQAS RGARSYANDI MLAKMIEALA AIYPEIPLCM HQDHGNNEAT CMTAIRHGFT SVMMDGSLKA DAKTPADYDY NVDITARVSH MAHWVGASVE GELGVLGSLE TGESEAEDGH GAEGKLDHSQ LLTDPDQAVD FVKKTQVDAL AIACGTSHGA YKFSRKPDGE ILAMSVIEAI HKKLPDTHLV MHGSSSVPQE LQDIINAFGG AMPQTFGVPV EEIVRGIKMG VRKVNIDTDC RMAMTGQFRR IAQQTPSEFD PRKFLKPAMD AMRDLCKQRL EAFGTAGQAG KIRIIPMDDM AKRYASGALA PKTA //