ID   ALDCB_DANRE             Reviewed;         363 AA.
AC   Q8JH70;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Fructose-bisphosphate aldolase C-B;
DE            EC=4.1.2.13;
DE   AltName: Full=Brain-type aldolase-B;
GN   Name=aldocb; Synonyms=aldoc;
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;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JUN-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   -!- 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; AF533647; AAN04478.1; -; mRNA.
DR   EMBL; BC053192; AAH53192.1; -; mRNA.
DR   RefSeq; NP_919365.1; NM_194384.1.
DR   AlphaFoldDB; Q8JH70; -.
DR   SMR; Q8JH70; -.
DR   STRING; 7955.ENSDARP00000024492; -.
DR   PaxDb; Q8JH70; -.
DR   PRIDE; Q8JH70; -.
DR   Ensembl; ENSDART00000026766; ENSDARP00000024492; ENSDARG00000019702.
DR   Ensembl; ENSDART00000183995; ENSDARP00000151215; ENSDARG00000019702.
DR   GeneID; 369193; -.
DR   KEGG; dre:369193; -.
DR   CTD; 369193; -.
DR   ZFIN; ZDB-GENE-030821-1; aldocb.
DR   eggNOG; KOG1557; Eukaryota.
DR   GeneTree; ENSGT00950000182987; -.
DR   HOGENOM; CLU_031243_0_0_1; -.
DR   InParanoid; Q8JH70; -.
DR   OMA; QKDNAGA; -.
DR   OrthoDB; 799973at2759; -.
DR   PhylomeDB; Q8JH70; -.
DR   TreeFam; TF314203; -.
DR   Reactome; R-DRE-6798695; Neutrophil degranulation.
DR   Reactome; R-DRE-70171; Glycolysis.
DR   Reactome; R-DRE-70263; Gluconeogenesis.
DR   UniPathway; UPA00109; UER00183.
DR   PRO; PR:Q8JH70; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 21.
DR   Bgee; ENSDARG00000019702; Expressed in bone element and 48 other tissues.
DR   ExpressionAtlas; Q8JH70; baseline.
DR   GO; GO:0005829; C:cytosol; 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   Glycolysis; Lyase; Reference proteome; Schiff base.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..363
FT                   /note="Fructose-bisphosphate aldolase C-B"
FT                   /id="PRO_0000291612"
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            363
FT                   /note="Necessary for preference for fructose 1,6-
FT                   bisphosphate over fructose 1-phosphate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   363 AA;  39259 MW;  84D269B36579E6A0 CRC64;
     MTHQYPALTA EQKKELQDIA QRIVAPGKGI LAADESTGSM AKRLNPIGVE NTEENRRLYR
     QLLFSADERI DKCIGGVIFF HETLYQNTDD GTNFAQLIKD RGIVVGIKVD KGVVPLAGTN
     GETTTQGLDG LSERCAQYKK DGADFAKWRS VLKISDTTPS ELAIMENANV LARYASICQQ
     NGIVPIVEPE ILPDGEHDLK RCQYVTEKVL AACYKALSDH HVYLEGTLLK PNMVTAGHSC
     PTKYSSEEIA MATVTALRRT VPPAVSGVTF LSGGQSEEEA SVNLNSINNC PLAKPWPLTF
     SYGRALQASA LSAWRGAKSN EKAATEEFIK RAEANGLAAQ GKYVSSGTCG AAGQSLYVAN
     HAY