ID   ALDOB_DANRE             Reviewed;         364 AA.
AC   Q8JH71;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Fructose-bisphosphate aldolase B;
DE            EC=4.1.2.13;
DE   AltName: Full=Liver-type aldolase;
GN   Name=aldob;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=12486526; DOI=10.1007/s00239-002-2363-8;
RA   Merritt T.J.S., Quattro J.M.;
RT   "Negative charge correlates with neural expression in vertebrate aldolase
RT   isozymes.";
RL   J. Mol. Evol. 55:674-683(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney marrow;
RX   PubMed=15520368; DOI=10.1073/pnas.0407241101;
RA   Song H.-D., Sun X.-J., Deng M., Zhang G.-W., Zhou Y., Wu X.-Y., Sheng Y.,
RA   Chen Y., Ruan Z., Jiang C.-L., Fan H.-Y., Zon L.I., Kanki J.P., Liu T.X.,
RA   Look A.T., Chen Z.;
RT   "Hematopoietic gene expression profile in zebrafish kidney marrow.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:16240-16245(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
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   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 4/4.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center, centrosome, centriolar satellite {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase
CC       family. {ECO:0000305}.
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DR   EMBL; AF533646; AAN04477.1; -; mRNA.
DR   EMBL; AY394965; AAQ94592.1; -; mRNA.
DR   EMBL; BC062830; AAH62830.1; -; mRNA.
DR   RefSeq; NP_919348.3; NM_194367.3.
DR   AlphaFoldDB; Q8JH71; -.
DR   SMR; Q8JH71; -.
DR   STRING; 7955.ENSDARP00000070225; -.
DR   PaxDb; Q8JH71; -.
DR   Ensembl; ENSDART00000075744; ENSDARP00000070225; ENSDARG00000053684.
DR   GeneID; 321664; -.
DR   KEGG; dre:321664; -.
DR   CTD; 229; -.
DR   ZFIN; ZDB-GENE-030131-383; aldob.
DR   eggNOG; KOG1557; Eukaryota.
DR   GeneTree; ENSGT00950000182987; -.
DR   HOGENOM; CLU_031243_0_0_1; -.
DR   InParanoid; Q8JH71; -.
DR   OMA; ANCQAAQ; -.
DR   OrthoDB; 799973at2759; -.
DR   PhylomeDB; Q8JH71; -.
DR   TreeFam; TF314203; -.
DR   Reactome; R-DRE-70171; Glycolysis.
DR   Reactome; R-DRE-70263; Gluconeogenesis.
DR   Reactome; R-DRE-70350; Fructose catabolism.
DR   UniPathway; UPA00109; UER00183.
DR   PRO; PR:Q8JH71; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 14.
DR   Bgee; ENSDARG00000053684; Expressed in liver and 39 other tissues.
DR   ExpressionAtlas; Q8JH71; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR   GO; GO:0061609; F:fructose-1-phosphate aldolase activity; IBA:GO_Central.
DR   GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IBA:GO_Central.
DR   GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IBA:GO_Central.
DR   GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR029768; Aldolase_I_AS.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR000741; FBA_I.
DR   PANTHER; PTHR11627; PTHR11627; 1.
DR   Pfam; PF00274; Glycolytic; 1.
DR   PROSITE; PS00158; ALDOLASE_CLASS_I; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Cytoskeleton; Glycolysis; Lyase; Reference proteome;
KW   Schiff base.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..364
FT                   /note="Fructose-bisphosphate aldolase B"
FT                   /id="PRO_0000291611"
FT   ACT_SITE        188
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        230
FT                   /note="Schiff-base intermediate with dihydroxyacetone-P"
FT                   /evidence="ECO:0000250"
FT   BINDING         56
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         147
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            364
FT                   /note="Necessary for preference for fructose 1,6-
FT                   bisphosphate over fructose 1-phosphate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   364 AA;  39288 MW;  FB2DD9CDDCF4DB9E CRC64;
     MTHQFPALST EQKKELATIA ERIVAPGKGI LAADESTGTM AKRFQKINVE NTEENRRSFR
     DLLFSVDDSI SESIGGVILF HETLYQKSDK GVLFPKVIKD KGIVVGIKVD KGTAGLAGTD
     GETTTQGLDG LSERCAQYKK DGCDFAKWRC VLKISDSCPS ALGIAENANV LARYASICQQ
     NGLVPIVEPE ILPDGDHDLK QCQYATEKVL AAVYKALSDH HVYLEGTLLK PNMVTAGHSC
     TKKYTPLEVA MATVTALRRT VPAAVPGICF LSGGQSEEEA SLNLNAMNQL SLHRPWKLSF
     SYGRALQASA LSAWKGQAAN KKASQDAFVT RAKINSLASK GEYKPSGQAG QASTQSLFTA
     SYTY