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ENOB_GADMO
ID   ENOB_GADMO              Reviewed;          11 AA.
AC   B3A0L6;
DT   22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT   22-JAN-2014, sequence version 1.
DT   03-AUG-2022, entry version 13.
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   AltName: Allergen=Gad m 2.0101 {ECO:0000303|PubMed:23786287};
DE   Flags: Fragment;
GN   Name=ENO3 {ECO:0000250|UniProtKB:P00924};
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, SUBUNIT, ALLERGEN, AND IDENTIFICATION BY MASS
RP   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:0000269|PubMed:23786287}.
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; 10147; Gad m 2.
DR   Allergome; 10148; Gad m 2.0101.
DR   UniPathway; UPA00109; UER00187.
DR   Proteomes; UP000694546; Unplaced.
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; Reference proteome.
FT   CHAIN           1..>11
FT                   /note="Beta-enolase"
FT                   /id="PRO_0000425075"
FT   NON_TER         11
FT                   /evidence="ECO:0000303|PubMed:23786287"
SQ   SEQUENCE   11 AA;  1272 MW;  507E30DB0DD33053 CRC64;
     SITKIKAREI L
 
 
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