ENOA_THUAL
ID ENOA_THUAL Reviewed; 432 AA.
AC I0J1J1; B3A0L7;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 03-AUG-2022, entry version 28.
DE RecName: Full=Alpha-enolase {ECO:0000250|UniProtKB:P04764};
DE EC=4.2.1.11 {ECO:0000250|UniProtKB:P00924};
DE AltName: Full=2-phospho-D-glycerate hydro-lyase {ECO:0000250|UniProtKB:P04764};
DE AltName: Full=Enolase 1 {ECO:0000250|UniProtKB:P04764};
DE AltName: Allergen=Thu a 2.0101 {ECO:0000303|PubMed:23786287};
GN Name=ENO1 {ECO:0000250|UniProtKB:P04764};
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:0000312|EMBL:CBL79145.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Muscle {ECO:0000312|EMBL:CBL79145.1};
RA Kuehn A., Hentges F.;
RT "Use of new fish allergen in diagnosis of fish allergy.";
RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 160-174, 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: Multifunctional enzyme that, as well as its role in
CC glycolysis, plays a part in various processes such as growth control,
CC hypoxia tolerance and allergic responses. {ECO:0000250}.
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:P00924};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds two Mg(2+) per subunit. Required for catalysis and for
CC stabilizing the dimer. {ECO:0000250};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 4/5. {ECO:0000250|UniProtKB:P00924}.
CC -!- SUBUNIT: Dimer. {ECO:0000250|UniProtKB:B5DGQ7}.
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 EMBL; FN812740; CBL79145.1; -; mRNA.
DR AlphaFoldDB; I0J1J1; -.
DR SMR; I0J1J1; -.
DR Allergome; 10132; Thu a 2.
DR UniPathway; UPA00109; UER00187.
DR GO; GO:0000015; C:phosphopyruvate hydratase complex; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004634; F:phosphopyruvate hydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR CDD; cd03313; enolase; 1.
DR Gene3D; 3.20.20.120; -; 1.
DR Gene3D; 3.30.390.10; -; 1.
DR HAMAP; MF_00318; Enolase; 1.
DR InterPro; IPR000941; Enolase.
DR InterPro; IPR036849; Enolase-like_C_sf.
DR InterPro; IPR029017; Enolase-like_N.
DR InterPro; IPR020810; Enolase_C.
DR InterPro; IPR020809; Enolase_CS.
DR InterPro; IPR020811; Enolase_N.
DR PANTHER; PTHR11902; PTHR11902; 1.
DR Pfam; PF00113; Enolase_C; 1.
DR Pfam; PF03952; Enolase_N; 1.
DR PIRSF; PIRSF001400; Enolase; 1.
DR PRINTS; PR00148; ENOLASE.
DR SFLD; SFLDF00002; enolase; 1.
DR SMART; SM01192; Enolase_C; 1.
DR SMART; SM01193; Enolase_N; 1.
DR SUPFAM; SSF51604; SSF51604; 1.
DR SUPFAM; SSF54826; SSF54826; 1.
DR TIGRFAMs; TIGR01060; eno; 1.
DR PROSITE; PS00164; ENOLASE; 1.
PE 1: Evidence at protein level;
KW Allergen; Cytoplasm; Direct protein sequencing; Glycolysis; Lyase;
KW Magnesium; Metal-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:B5DGQ7"
FT CHAIN 2..432
FT /note="Alpha-enolase"
FT /evidence="ECO:0000250|UniProtKB:P00924"
FT /id="PRO_0000425078"
FT ACT_SITE 210
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P00924"
FT ACT_SITE 343
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P00924"
FT BINDING 40
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 158
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00924"
FT BINDING 167
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00924"
FT BINDING 245
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 293
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 293
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00924"
FT BINDING 318
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 318
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00924"
FT BINDING 370..373
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00924"
FT BINDING 394
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00924"
SQ SEQUENCE 432 AA; 47136 MW; 331D80F26AA76D82 CRC64;
MSILKIHARE IFDSRGNPTV EVDLYTKKGL FRAAVPSGAS TGIYEALELR DNDKTRYMGK
GVKRAVKYIN EFLAPALCNQ DVTVIEQEKI DKLMLDMDGT ENKYKFGANA ILGVSLAVCK
AGAAEKGVPL YRHIADLAGN PEVILPVPAF NVINGGSHAG NKLAMQEFMI LPVGASSFKD
AMRIGAEVYH NLKNVIKEKY GKDATNVGDE GGFAPNILEN KEALKLLKNA IGKAGYTDKI
VIGMDVAASE FYKGGKYDLD FKSPDDPSRY IPSDKLADLY KGFVKDYPVV SIEDPFDQDD
WEAWSKFTAS TSIQVVGDDL TVTNPKRIAK GVAEKSCNCL LLKVNQIGSV TESLQACKMA
QSSGWGVMVS HRSGETEDTL ISDLVVGLCT GQIKTGAPCR SERLAKYNQL MRIEEELGAK
AKFAGKNFRH PI
