ID   ALDOB_RAT               Reviewed;         364 AA.
AC   P00884; P70706;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   08-NOV-2023, entry version 159.
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   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=6094564; DOI=10.1016/s0021-9258(17)42639-1;
RA   Tsutsumi K., Mukai T., Tsutsumi R., Mori M., Daimon M., Tanaka T.,
RA   Yatsuki H., Hori K., Ishikawa K.;
RT   "Nucleotide sequence of rat liver aldolase B messenger RNA.";
RL   J. Biol. Chem. 259:14572-14575(1984).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Sprague-Dawley;
RX   PubMed=2580098; DOI=10.1016/0022-2836(85)90081-6;
RA   Tsutsumi K., Mukai T., Tsutsumi R., Hidaka S., Arai Y., Hori K.,
RA   Ishikawa K.;
RT   "Structure and genomic organization of the rat aldolase B gene.";
RL   J. Mol. Biol. 181:153-160(1985).
RN   [3]
RP   NUCLEOTIDE SEQUENCE OF 185-364.
RX   PubMed=6304044; DOI=10.1016/s0021-9258(18)32445-1;
RA   Tsutsumi K., Mukai T., Hidaka S., Miyahara H., Tsutsumi R., Tanaka T.,
RA   Hori K., Ishikawa K.;
RT   "Rat aldolase isozyme gene.";
RL   J. Biol. Chem. 258:6537-6542(1983).
RN   [4]
RP   PROTEIN SEQUENCE OF 41-68.
RX   PubMed=1834654; DOI=10.1016/s0021-9258(18)54808-0;
RA   Brand I.A., Heinickel A.;
RT   "Key enzymes of carbohydrate metabolism as targets of the 11.5-kDa Zn(2+)-
RT   binding protein (parathymosin).";
RL   J. Biol. Chem. 266:20984-20989(1991).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36; THR-39; SER-132; SER-299
RP   AND SER-301, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
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; M10149; AAA40716.1; -; mRNA.
DR   EMBL; X02284; CAA26156.1; -; Genomic_DNA.
DR   EMBL; X02285; CAA26156.1; JOINED; Genomic_DNA.
DR   EMBL; X02286; CAA26156.1; JOINED; Genomic_DNA.
DR   EMBL; X02287; CAA26156.1; JOINED; Genomic_DNA.
DR   EMBL; X02288; CAA26156.1; JOINED; Genomic_DNA.
DR   EMBL; X02289; CAA26156.1; JOINED; Genomic_DNA.
DR   EMBL; X02290; CAA26156.1; JOINED; Genomic_DNA.
DR   EMBL; X02291; CAA26156.1; JOINED; Genomic_DNA.
DR   EMBL; V01223; CAA24533.1; -; mRNA.
DR   PIR; A22585; ADRTB.
DR   AlphaFoldDB; P00884; -.
DR   SMR; P00884; -.
DR   IntAct; P00884; 1.
DR   MINT; P00884; -.
DR   STRING; 10116.ENSRNOP00000009111; -.
DR   iPTMnet; P00884; -.
DR   PhosphoSitePlus; P00884; -.
DR   jPOST; P00884; -.
DR   PaxDb; 10116-ENSRNOP00000009111; -.
DR   UCSC; RGD:2090; rat.
DR   AGR; RGD:2090; -.
DR   RGD; 2090; Aldob.
DR   eggNOG; KOG1557; Eukaryota.
DR   InParanoid; P00884; -.
DR   PhylomeDB; P00884; -.
DR   BRENDA; 4.1.2.13; 5301.
DR   Reactome; R-RNO-70171; Glycolysis.
DR   Reactome; R-RNO-70263; Gluconeogenesis.
DR   Reactome; R-RNO-70350; Fructose catabolism.
DR   SABIO-RK; P00884; -.
DR   UniPathway; UPA00109; UER00183.
DR   UniPathway; UPA00138; -.
DR   UniPathway; UPA00202; -.
DR   PRO; PR:P00884; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0034451; C:centriolar satellite; ISO:RGD.
DR   GO; GO:0005829; C:cytosol; ISO:RGD.
DR   GO; GO:0005815; C:microtubule organizing center; ISO:RGD.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR   GO; GO:0030867; C:rough endoplasmic reticulum membrane; IDA:RGD.
DR   GO; GO:0030868; C:smooth endoplasmic reticulum membrane; IDA:RGD.
DR   GO; GO:0051117; F:ATPase binding; ISO:RGD.
DR   GO; GO:0008092; F:cytoskeletal protein binding; ISO:RGD.
DR   GO; GO:0070061; F:fructose binding; ISO:RGD.
DR   GO; GO:0061609; F:fructose-1-phosphate aldolase activity; ISS:UniProtKB.
DR   GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IDA:RGD.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR   GO; GO:0060090; F:molecular adaptor activity; ISO:RGD.
DR   GO; GO:0031210; F:phosphatidylcholine binding; IPI:RGD.
DR   GO; GO:0031668; P:cellular response to extracellular stimulus; IEP:RGD.
DR   GO; GO:0032869; P:cellular response to insulin stimulus; IEP:RGD.
DR   GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; ISO:RGD.
DR   GO; GO:0006001; P:fructose catabolic process; ISO:RGD.
DR   GO; GO:0061624; P:fructose catabolic process to hydroxyacetone phosphate and glyceraldehyde-3-phosphate; ISO:RGD.
DR   GO; GO:0006000; P:fructose metabolic process; ISO:RGD.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006096; P:glycolytic process; ISS:UniProtKB.
DR   GO; GO:0001889; P:liver development; IEP:RGD.
DR   GO; GO:0006116; P:NADH oxidation; ISO:RGD.
DR   GO; GO:1905856; P:negative regulation of pentose-phosphate shunt; ISO:RGD.
DR   GO; GO:0043200; P:response to amino acid; IEP:RGD.
DR   GO; GO:0051591; P:response to cAMP; IEP:RGD.
DR   GO; GO:0009743; P:response to carbohydrate; IEP:RGD.
DR   GO; GO:0046688; P:response to copper ion; IEP:RGD.
DR   GO; GO:0009750; P:response to fructose; IEP:RGD.
DR   GO; GO:0051384; P:response to glucocorticoid; IEP:RGD.
DR   GO; GO:0070741; P:response to interleukin-6; IEP:RGD.
DR   GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR   GO; GO:0043434; P:response to peptide hormone; IDA:RGD.
DR   GO; GO:0042594; P:response to starvation; IEP:RGD.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR   GO; GO:0010043; P:response to zinc ion; IDA:RGD.
DR   GO; GO:0070072; P:vacuolar proton-transporting V-type ATPase complex assembly; ISO:RGD.
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   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW   Glycolysis; Lyase; Phosphoprotein; 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_0000216943"
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:0007744|PubMed:22673903"
FT   MOD_RES         39
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         89
FT                   /note="Phosphoserine"
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:0007744|PubMed:22673903"
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:0007744|PubMed:22673903"
FT   MOD_RES         301
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
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"
FT   CONFLICT        234
FT                   /note="L -> V (in Ref. 2; CAA26156)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   364 AA;  39618 MW;  E120FC119F0180F8 CRC64;
     MAHRFPALTS EQKKELSEIA QRIVANGKGI LAADESVGTM GNRLQRIKVE NTEENRRQFR
     ELLFSVDNSI SQSIGGVILF HETLYQKDSQ GKLFRNILKE KGIVVGIKLD QGGAPLAGTN
     KETTIQGLDG LSERCAQYKK DGVDFGKWRA VLRISDQCPS SLAIQENANA LARYASICQQ
     NGLVPIVEPE VLPDGDHDLE HCQYVSEKVL AAVYKALNDH HVYLEGTLLK PNMLTAGHAC
     TKKYTPEQVA MATVTALHRT VPAAVPSICF LSGGMSEEDA TLNLNAIYRC PLPRPWKLSF
     SYGRALQASA LAAWGGKAAN KKATQEAFMK RAVANCQAAQ GQYVHTGSSG AASTQSLFTA
     SYTY
//