ID   ALDOA_GADMO             Reviewed;          15 AA.
AC   P86980;
DT   22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT   22-JAN-2014, sequence version 1.
DT   03-AUG-2022, entry version 10.
DE   RecName: Full=Fructose-bisphosphate aldolase A {ECO:0000303|PubMed:23786287};
DE            EC=4.1.2.13 {ECO:0000250|UniProtKB:P00883};
DE   AltName: Full=Muscle-type aldolase {ECO:0000250|UniProtKB:P00883};
DE   AltName: Allergen=Gad m 3.0101 {ECO:0000303|PubMed:23786287};
DE   Flags: Fragment;
GN   Name=ALDOA {ECO:0000250|UniProtKB:P00883};
OS   Gadus morhua (Atlantic cod).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Zeiogadaria; Gadariae; Gadiformes; Gadoidei; Gadidae; Gadus.
OX   NCBI_TaxID=8049;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, ALLERGEN, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Muscle {ECO:0000269|PubMed:23786287};
RX   PubMed=23786287; DOI=10.1111/cea.12117;
RA   Kuehn A., Hilger C., Lehners-Weber C., Codreanu-Morel F., Morisset M.,
RA   Metz-Favre C., Pauli G., de Blay F., Revets D., Muller C.P., Vogel L.,
RA   Vieths S., Hentges F.;
RT   "Identification of enolases and aldolases as important fish allergens in
RT   cod, salmon and tuna: component resolved diagnosis using parvalbumin and
RT   the new allergens.";
RL   Clin. Exp. Allergy 43:811-822(2013).
CC   -!- FUNCTION: Plays a key role in glycolysis and gluconeogenesis.
CC       {ECO:0000250|UniProtKB:P00883}.
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:P04075};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14730;
CC         Evidence={ECO:0000250|UniProtKB:P04075};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 4/4.
CC       {ECO:0000250|UniProtKB:P00883}.
CC   -!- SUBUNIT: Tetramer. {ECO:0000250|UniProtKB:P00883}.
CC   -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE.
CC       {ECO:0000269|PubMed:23786287}.
CC   -!- MISCELLANEOUS: In vertebrates, three forms of this ubiquitous
CC       glycolytic enzyme are found, aldolase A in muscle, aldolase B in liver
CC       and aldolase C in brain. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase
CC       family. {ECO:0000255}.
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DR   STRING; 8049.ENSGMOP00000010396; -.
DR   Allergome; 10149; Gad m 3.
DR   Allergome; 10150; Gad m 3.0101.
DR   UniPathway; UPA00109; UER00183.
DR   Proteomes; UP000694546; Unplaced.
DR   GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
PE   1: Evidence at protein level;
KW   Allergen; Direct protein sequencing; Glycolysis; Lyase; Reference proteome.
FT   CHAIN           1..>15
FT                   /note="Fructose-bisphosphate aldolase A"
FT                   /id="PRO_0000425072"
FT   NON_TER         15
FT                   /evidence="ECO:0000303|PubMed:23786287"
SQ   SEQUENCE   15 AA;  1784 MW;  9601886D0B852A65 CRC64;
     PHAYPFLSPE QKKEL