ID   ALDOC_CARAU             Reviewed;         363 AA.
AC   P53448;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Fructose-bisphosphate aldolase C;
DE            EC=4.1.2.13;
DE   AltName: Full=Brain-type aldolase;
GN   Name=aldoc;
OS   Carassius auratus (Goldfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Cyprininae; Carassius.
OX   NCBI_TaxID=7957;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Brain;
RX   PubMed=9219352; DOI=10.1016/s0300-9629(96)00396-9;
RA   Berardini T.Z., Drygas-Williams M., Callard G.V., Tolan D.R.;
RT   "Identification of neuronal isozyme specific residues by comparison of
RT   goldfish aldolase C to other aldolases.";
RL   Comp. Biochem. Physiol. 117A:471-476(1997).
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   -!- TISSUE SPECIFICITY: Expressed in brain but not in liver or muscle.
CC       {ECO:0000269|PubMed:9219352}.
CC   -!- SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase
CC       family. {ECO:0000305}.
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DR   EMBL; U36777; AAA84887.1; -; mRNA.
DR   AlphaFoldDB; P53448; -.
DR   SMR; P53448; -.
DR   UniPathway; UPA00109; UER00183.
DR   Proteomes; UP000515129; Genome assembly.
DR   GO; GO:0004332; F:fructose-bisphosphate aldolase activity; ISS:UniProtKB.
DR   GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; ISS:UniProtKB.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
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"
FT                   /id="PRO_0000216953"
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;  39475 MW;  23ED53BABED42327 CRC64;
     MTHQYPALTT EQKRELQDIA QRIVAPGKGI LAADESTGSM AKRLNPIGVE NTEENRRLYR
     QLLFTADERM DKCIGGVIFF HETLYQKADD GTPFAKMIKD RGIVVGIKVD KGVVPLAGTN
     GETTTQGLDG LSERCAQYKK DGADFAKWRS VLKISETSPS ELAIMENANV LARYASICQQ
     NGIVPIVEPE ILPDGDHDLK RCQYVTEKVL AACYKALSDH HVYLEGTLLK PNMVTAGHSC
     PTKFSNQEIA MATVTALRRT VPPAVTGVTF LSGGQSEEEA SINLNAINNC PLTKPWALTF
     SYGRALQASA LSAWRGVKEN EKAATEEFLK RAEANGLAAQ GKYVSSGMDG SAGQSLYVAN
     HAY