ENOB_THUAL
ID ENOB_THUAL Reviewed; 12 AA.
AC P86978;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 22-JAN-2014, sequence version 1.
DT 23-FEB-2022, entry version 12.
DE RecName: Full=Beta-enolase {ECO:0000303|PubMed:23786287};
DE EC=4.2.1.11 {ECO:0000250|UniProtKB:P00924};
DE AltName: Full=2-phospho-D-glycerate hydro-lyase {ECO:0000250|UniProtKB:P21550};
DE AltName: Full=Enolase 3 {ECO:0000250|UniProtKB:P21550};
DE AltName: Full=Muscle-specific enolase {ECO:0000250|UniProtKB:P21550};
DE Short=MSE {ECO:0000250|UniProtKB:P21550};
DE AltName: Full=Skeletal muscle enolase {ECO:0000250|UniProtKB:P21550};
DE Flags: Fragment;
GN Name=ENO3 {ECO:0000250|UniProtKB:P21550};
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: Glycolytic enzyme that catalyzes the conversion of 2-
CC phosphoglycerate to phosphoenolpyruvate.
CC {ECO:0000250|UniProtKB:P15429}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate;
CC Xref=Rhea:RHEA:10164, ChEBI:CHEBI:15377, ChEBI:CHEBI:58289,
CC ChEBI:CHEBI:58702; EC=4.2.1.11;
CC Evidence={ECO:0000250|UniProtKB:P15429};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10165;
CC Evidence={ECO:0000250|UniProtKB:P15429};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P00924};
CC Note=Mg(2+) is required for catalysis and for stabilizing the dimer.
CC {ECO:0000250|UniProtKB:P00924};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 4/5. {ECO:0000250|UniProtKB:P15429}.
CC -!- SUBUNIT: Dimer. {ECO:0000250|UniProtKB:B3A0L6}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P00924}.
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE.
CC {ECO:0000269|PubMed:23786287}.
CC -!- SIMILARITY: Belongs to the enolase family. {ECO:0000255}.
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DR Allergome; 10132; Thu a 2.
DR Allergome; 10153; Thu a 2.0101.
DR UniPathway; UPA00109; UER00187.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004634; F:phosphopyruvate hydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
PE 1: Evidence at protein level;
KW Allergen; Cytoplasm; Direct protein sequencing; Glycolysis; Lyase;
KW Magnesium; Metal-binding.
FT CHAIN 1..>12
FT /note="Beta-enolase"
FT /id="PRO_0000425077"
FT NON_TER 12
FT /evidence="ECO:0000303|PubMed:23786287"
SQ SEQUENCE 12 AA; 1387 MW; 1F407E30DB0DD330 CRC64;
SITKIKAREI LD
