ALDOA_THUAL
ID ALDOA_THUAL Reviewed; 37 AA.
AC P86979;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 22-JAN-2014, sequence version 1.
DT 25-MAY-2022, entry version 12.
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=Thu a 3.0101 {ECO:0000303|PubMed:23786287};
DE Flags: Fragment;
GN Name=ALDOA {ECO:0000250|UniProtKB:P00883};
OS Thunnus albacares (Yellowfin tuna) (Neothunnus macropterus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Pelagiaria; Scombriformes; Scombridae; Thunnus.
OX NCBI_TaxID=8236;
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 AlphaFoldDB; P86979; -.
DR SMR; P86979; -.
DR Allergome; 10154; Thu a 3.
DR Allergome; 10155; Thu a 3.0101.
DR UniPathway; UPA00109; UER00183.
DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:UniProtKB-EC.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000741; FBA_I.
DR Pfam; PF00274; Glycolytic; 1.
PE 1: Evidence at protein level;
KW Allergen; Direct protein sequencing; Glycolysis; Lyase.
FT CHAIN 1..>37
FT /note="Fructose-bisphosphate aldolase A"
FT /id="PRO_0000425074"
FT NON_TER 37
FT /evidence="ECO:0000303|PubMed:23786287"
SQ SEQUENCE 37 AA; 3914 MW; 90BCFDE3A13AF91B CRC64;
PHAFPFLTPE QKKELSDIAH KIVAPGKGIL AADESTG
