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}.
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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
//
