ID ALDOB_SHEEP Reviewed; 364 AA. AC P52210; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 24-JAN-2024, entry version 106. DE RecName: Full=Fructose-bisphosphate aldolase B; DE EC=4.1.2.13 {ECO:0000250|UniProtKB:P05062}; DE AltName: Full=Liver-type aldolase; GN Name=ALDOB; OS Ovis aries (Sheep). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Caprinae; Ovis. OX NCBI_TaxID=9940; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Mesonephros; RX PubMed=8086469; DOI=10.1016/0167-4781(94)90277-1; RA Gianquinto L., Pailhoux E.A., Bezard J., Servel N., Kirszenbaum M., RA Cotinot C.; RT "Cloning and characterization of a full-length cDNA coding for ovine RT aldolase B from fetal mesonephros."; RL Biochim. Biophys. Acta 1219:223-227(1994). CC -!- FUNCTION: Catalyzes the aldol cleavage of fructose 1,6-biphosphate to CC form two triosephosphates dihydroxyacetone phosphate and D- CC glyceraldehyde 3-phosphate in glycolysis as well as the reverse CC stereospecific aldol addition reaction in gluconeogenesis. In CC fructolysis, metabolizes fructose 1-phosphate derived from the CC phosphorylation of dietary fructose by fructokinase into CC dihydroxyacetone phosphate and D-glyceraldehyde (By similarity). Acts CC as an adapter independently of its enzymatic activity, exerts a tumor CC suppressor role by stabilizing the ternary complex with G6PD and TP53 CC to inhibit G6PD activity and keep oxidative pentose phosphate CC metabolism in check (By similarity). {ECO:0000250|UniProtKB:P05062}. 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 Evidence={ECO:0000250|UniProtKB:P05062}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14730; CC Evidence={ECO:0000250|UniProtKB:P05062}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:14731; CC Evidence={ECO:0000250|UniProtKB:P05062}; CC -!- CATALYTIC ACTIVITY: CC Reaction=beta-D-fructose 1-phosphate = D-glyceraldehyde + CC dihydroxyacetone phosphate; Xref=Rhea:RHEA:30851, ChEBI:CHEBI:17378, CC ChEBI:CHEBI:57642, ChEBI:CHEBI:138881; CC Evidence={ECO:0000250|UniProtKB:P05062}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30852; CC Evidence={ECO:0000250|UniProtKB:P05062}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:30853; CC Evidence={ECO:0000250|UniProtKB:P05062}; CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- CC phosphate and glycerone phosphate from D-glucose: step 4/4. CC {ECO:0000250|UniProtKB:P05062}. CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. CC {ECO:0000250|UniProtKB:P05062}. CC -!- PATHWAY: Carbohydrate metabolism; fructose metabolism. CC {ECO:0000250|UniProtKB:P05062}. CC -!- SUBUNIT: Homotetramer. Interacts with BBS1, BBS2, BBS4 and BBS7. Forms CC a ternary complex with G6PD and TP53; this interaction is direct. CC {ECO:0000250|UniProtKB:P05062}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol CC {ECO:0000250|UniProtKB:P05062}. Cytoplasm, cytoskeleton, microtubule CC organizing center, centrosome, centriolar satellite CC {ECO:0000250|UniProtKB:P05062}. CC -!- MISCELLANEOUS: In vertebrates, 3 forms of this ubiquitous glycolytic CC enzyme are found, aldolase A in muscle, aldolase B in liver and CC aldolase C in brain. CC -!- SIMILARITY: Belongs to the class I 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; Z29372; CAA82563.1; -; mRNA. DR PIR; S47540; S47540. DR RefSeq; NP_001009809.1; NM_001009809.1. DR AlphaFoldDB; P52210; -. DR SMR; P52210; -. DR STRING; 9940.ENSOARP00000008061; -. DR PaxDb; 9940-ENSOARP00000008061; -. DR GeneID; 443440; -. DR KEGG; oas:443440; -. DR CTD; 229; -. DR eggNOG; KOG1557; Eukaryota. DR OrthoDB; 3664741at2759; -. DR UniPathway; UPA00109; UER00183. DR UniPathway; UPA00138; -. DR UniPathway; UPA00202; -. DR Proteomes; UP000002356; Unplaced. DR GO; GO:0034451; C:centriolar satellite; IEA:UniProtKB-SubCell. DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell. DR GO; GO:0061609; F:fructose-1-phosphate aldolase activity; ISS:UniProtKB. DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; ISS:UniProtKB. DR GO; GO:0006000; P:fructose metabolic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway. DR GO; GO:0006096; P:glycolytic process; ISS:UniProtKB. DR CDD; cd00948; FBP_aldolase_I_a; 1. DR Gene3D; 3.20.20.70; Aldolase class I; 1. DR InterPro; IPR029768; Aldolase_I_AS. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000741; FBA_I. DR NCBIfam; NF033379; FrucBisAld_I; 1. DR PANTHER; PTHR11627; FRUCTOSE-BISPHOSPHATE ALDOLASE; 1. DR PANTHER; PTHR11627:SF2; FRUCTOSE-BISPHOSPHATE ALDOLASE B; 1. DR Pfam; PF00274; Glycolytic; 1. DR SUPFAM; SSF51569; Aldolase; 1. DR PROSITE; PS00158; ALDOLASE_CLASS_I; 1. PE 2: Evidence at transcript level; KW Acetylation; Cytoplasm; Cytoskeleton; Glycolysis; Lyase; Phosphoprotein; KW Reference proteome; Schiff base. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:Q91Y97" FT CHAIN 2..364 FT /note="Fructose-bisphosphate aldolase B" FT /id="PRO_0000216944" FT ACT_SITE 188 FT /note="Proton acceptor" FT /evidence="ECO:0000250|UniProtKB:P00883" FT ACT_SITE 230 FT /note="Schiff-base intermediate with dihydroxyacetone-P" FT /evidence="ECO:0000250|UniProtKB:P00883" FT BINDING 43 FT /ligand="beta-D-fructose 1,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:32966" FT /evidence="ECO:0000250|UniProtKB:P00883" FT BINDING 272..274 FT /ligand="beta-D-fructose 1,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:32966" FT /evidence="ECO:0000250|UniProtKB:P00883" FT BINDING 304 FT /ligand="beta-D-fructose 1,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:32966" FT /evidence="ECO:0000250|UniProtKB:P00883" FT SITE 364 FT /note="Necessary for preference for fructose 1,6- FT bisphosphate over fructose 1-phosphate" FT /evidence="ECO:0000250|UniProtKB:P00883" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000250|UniProtKB:Q91Y97" FT MOD_RES 13 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q91Y97" FT MOD_RES 36 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P05062" FT MOD_RES 39 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P05062" FT MOD_RES 119 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P05062" FT MOD_RES 121 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q91Y97" FT MOD_RES 132 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P05062" FT MOD_RES 272 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P05062" FT MOD_RES 276 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P05062" FT MOD_RES 299 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P00884" FT MOD_RES 301 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P00884" FT MOD_RES 309 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P05062" FT MOD_RES 317 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q91Y97" SQ SEQUENCE 364 AA; 39631 MW; 935F4A91D6C6BFDF CRC64; MAHQFPALTS EQKKALSETA RRIVANGKGI LAADESVGTM GNRLQRIKVE NTEENRRQFR ELLFTVDSSV SQSIGGVILF HETLYQKDGQ GKLFRDILKE KGIVVGIKLD QGVAPLAGTN KETTVQGLDG LSERCAQYKK DGADFGKWRA VLKIDNQCPS HLAIQENANT LARYASIYQQ NGLVPIVEPE VIPDGSHDME HCQYVTEKVL AAVYKALNDH HVYLEGTLLK PNMVTAGHAC TKKYTPEQVA MATVTALHRT VPAAVPGICF LSGGMSEEDA TLNLNAINLC PLPKPWKLSF SYGRALQASA LAAWGGKAEN KKATQEAFMK RALANSQAAK GQYVHMGSSD SASTQSLFTA SYTY //