ID   ALDOB_RABIT             Reviewed;         364 AA.
AC   P79226;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   24-JAN-2024, entry version 140.
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; Synonyms=ALDB;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10327593; DOI=10.1016/s0305-0491(98)10140-2;
RA   Berardini T.Z., Amsden A.B., Penhoet E.E., Tolan D.R.;
RT   "Identification of conserved promoter elements for aldB and isozyme
RT   specific residues in aldolase B.";
RL   Comp. Biochem. Physiol. 122B:53-61(1999).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
RX   PubMed=9761929; DOI=10.1107/s0907444997006549;
RA   Blom N., Sygush J.;
RT   "Enhanced electron-density envelopes by extended solvent definition.";
RL   Acta Crystallogr. D 54:461-466(1998).
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; U85645; AAB42087.1; -; Genomic_DNA.
DR   PIR; A28856; A28856.
DR   RefSeq; NP_001164585.1; NM_001171114.1.
DR   PDB; 1FDJ; X-ray; 2.10 A; A/B/C/D=2-364.
DR   PDBsum; 1FDJ; -.
DR   AlphaFoldDB; P79226; -.
DR   SMR; P79226; -.
DR   STRING; 9986.ENSOCUP00000002717; -.
DR   iPTMnet; P79226; -.
DR   PaxDb; 9986-ENSOCUP00000012843; -.
DR   Ensembl; ENSOCUT00000014943.3; ENSOCUP00000012843.2; ENSOCUG00000014944.3.
DR   GeneID; 100328925; -.
DR   KEGG; ocu:100328925; -.
DR   CTD; 229; -.
DR   eggNOG; KOG1557; Eukaryota.
DR   GeneTree; ENSGT00950000182987; -.
DR   HOGENOM; CLU_031243_0_0_1; -.
DR   InParanoid; P79226; -.
DR   OMA; ANCQAAQ; -.
DR   OrthoDB; 3664741at2759; -.
DR   TreeFam; TF314203; -.
DR   SABIO-RK; P79226; -.
DR   UniPathway; UPA00109; UER00183.
DR   UniPathway; UPA00138; -.
DR   UniPathway; UPA00202; -.
DR   EvolutionaryTrace; P79226; -.
DR   Proteomes; UP000001811; Chromosome 1.
DR   Bgee; ENSOCUG00000014944; Expressed in adult mammalian kidney and 16 other cell types or tissues.
DR   ExpressionAtlas; P79226; baseline.
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   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cytoplasm; Cytoskeleton; Glycolysis; Lyase;
KW   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_0000216942"
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         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: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"
FT   HELIX           10..24
FT                   /evidence="ECO:0007829|PDB:1FDJ"
FT   HELIX           25..27
FT                   /evidence="ECO:0007829|PDB:1FDJ"
FT   STRAND          29..33
FT                   /evidence="ECO:0007829|PDB:1FDJ"
FT   HELIX           37..46
FT                   /evidence="ECO:0007829|PDB:1FDJ"
FT   HELIX           53..64
FT                   /evidence="ECO:0007829|PDB:1FDJ"
FT   HELIX           68..72
FT                   /evidence="ECO:0007829|PDB:1FDJ"
FT   STRAND          74..79
FT                   /evidence="ECO:0007829|PDB:1FDJ"
FT   HELIX           81..84
FT                   /evidence="ECO:0007829|PDB:1FDJ"
FT   HELIX           94..100
FT                   /evidence="ECO:0007829|PDB:1FDJ"
FT   STRAND          104..108
FT                   /evidence="ECO:0007829|PDB:1FDJ"
FT   STRAND          113..115
FT                   /evidence="ECO:0007829|PDB:1FDJ"
FT   STRAND          119..121
FT                   /evidence="ECO:0007829|PDB:1FDJ"
FT   STRAND          123..125
FT                   /evidence="ECO:0007829|PDB:1FDJ"
FT   HELIX           131..140
FT                   /evidence="ECO:0007829|PDB:1FDJ"
FT   STRAND          145..152
FT                   /evidence="ECO:0007829|PDB:1FDJ"
FT   HELIX           161..180
FT                   /evidence="ECO:0007829|PDB:1FDJ"
FT   STRAND          184..191
FT                   /evidence="ECO:0007829|PDB:1FDJ"
FT   HELIX           199..219
FT                   /evidence="ECO:0007829|PDB:1FDJ"
FT   HELIX           224..226
FT                   /evidence="ECO:0007829|PDB:1FDJ"
FT   HELIX           246..258
FT                   /evidence="ECO:0007829|PDB:1FDJ"
FT   STRAND          267..270
FT                   /evidence="ECO:0007829|PDB:1FDJ"
FT   HELIX           277..289
FT                   /evidence="ECO:0007829|PDB:1FDJ"
FT   STRAND          296..303
FT                   /evidence="ECO:0007829|PDB:1FDJ"
FT   HELIX           304..314
FT                   /evidence="ECO:0007829|PDB:1FDJ"
FT   HELIX           318..320
FT                   /evidence="ECO:0007829|PDB:1FDJ"
FT   HELIX           321..338
FT                   /evidence="ECO:0007829|PDB:1FDJ"
FT   TURN            339..341
FT                   /evidence="ECO:0007829|PDB:1FDJ"
FT   STRAND          353..357
FT                   /evidence="ECO:0007829|PDB:1FDJ"
SQ   SEQUENCE   364 AA;  39605 MW;  65A58A50906EA954 CRC64;
     MAHRFPALTP EQKKELSDIA QRIVANGKGI LAADESVGTM GNRLQRIKVE NTEENRRQFR
     EILFTVDNSI NQSIGGVILF HETLYQKDSQ GKLFRNILKE KGIVVGIKLD QGGAPLAGTN
     KETTIQGLDG LSERCAQYKK DGVDFGKWRA VLRIADQCPS SLAIQENANT LARYASICQQ
     NGLVPIVEPE VIPDGDHDLE HCQYVTEKVL AAVYKALNDH HVYLEGTLLK PNMVTAGHAC
     TKKYTPEQVA MATVTALHRT VPAAVPGICF LSGGMSEEDA TLNLNAINLC PLPKPWKLSF
     SYGRALQASA LAAWGGKAEN KKATQEAFMK RAVVNCQAAK GQYVHTGSSG AASTQSLFTA
     SYTY
//