ENOB_SALSA
ID ENOB_SALSA Reviewed; 434 AA.
AC B5DGQ7; B5DGQ6;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 03-AUG-2022, entry version 52.
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=Sal s 2.0101 {ECO:0000303|PubMed:23786287};
GN Name=ENO3 {ECO:0000250|UniProtKB:P21550};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030;
RN [1] {ECO:0000312|EMBL:ACH70931.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=White muscle {ECO:0000312|EMBL:ACH70931.1};
RX PubMed=19878547; DOI=10.1186/1471-2164-10-502;
RA Andreassen R., Lunner S., Hoyheim B.;
RT "Characterization of full-length sequenced cDNA inserts (FLIcs) from
RT Atlantic salmon (Salmo salar).";
RL BMC Genomics 10:502-502(2009).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 2-13, 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: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 EMBL; BT043815; ACH70930.1; -; mRNA.
DR EMBL; BT043816; ACH70931.1; -; mRNA.
DR EMBL; BT043817; ACH70932.1; -; mRNA.
DR RefSeq; NP_001133193.1; NM_001139721.1.
DR RefSeq; NP_001135172.1; NM_001141700.1.
DR AlphaFoldDB; B5DGQ7; -.
DR SMR; B5DGQ7; -.
DR STRING; 8030.ENSSSAP00000041541; -.
DR Allergome; 9699; Sal s 2.
DR Allergome; 9700; Sal s 2.0101.
DR GeneID; 100194636; -.
DR GeneID; 100196671; -.
DR KEGG; sasa:100194636; -.
DR KEGG; sasa:100196671; -.
DR CTD; 2027; -.
DR OrthoDB; 773373at2759; -.
DR UniPathway; UPA00109; UER00187.
DR Proteomes; UP000087266; Chromosome ssa18.
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; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:23786287"
FT CHAIN 2..434
FT /note="Beta-enolase"
FT /evidence="ECO:0000269|PubMed:23786287"
FT /id="PRO_0000425076"
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 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 /evidence="ECO:0000250|UniProtKB:P00924"
FT BINDING 293
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00924"
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 /evidence="ECO:0000250|UniProtKB:P00924"
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"
FT CONFLICT 4
FT /note="T -> I (in Ref. 1; ACH70930)"
FT /evidence="ECO:0000305"
FT CONFLICT 43
FT /note="V -> I (in Ref. 1; ACH70930)"
FT /evidence="ECO:0000305"
FT CONFLICT 63
FT /note="V -> L (in Ref. 1; ACH70930)"
FT /evidence="ECO:0000305"
FT CONFLICT 92
FT /note="H -> K (in Ref. 1; ACH70930)"
FT /evidence="ECO:0000305"
FT CONFLICT 131
FT /note="Y -> F (in Ref. 1; ACH70930)"
FT /evidence="ECO:0000305"
FT CONFLICT 229
FT /note="T -> S (in Ref. 1; ACH70930)"
FT /evidence="ECO:0000305"
FT CONFLICT 305
FT /note="T -> S (in Ref. 1; ACH70930)"
FT /evidence="ECO:0000305"
FT CONFLICT 416
FT /note="E -> A (in Ref. 1; ACH70930)"
FT /evidence="ECO:0000305"
FT CONFLICT 419
FT /note="A -> D (in Ref. 1; ACH70930)"
FT /evidence="ECO:0000305"
FT CONFLICT 433
FT /note="I -> V (in Ref. 1; ACH70930)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 434 AA; 47287 MW; 802A7956054679B5 CRC64;
MSITKIHARE ILDSRGNPTV EVDLYTAKGR FRAAVPSGAS TGVHEALELR DGDKSRYLGK
GTVKAVDHVN KDIAAKLIEK KFSVVDQEKI DHFMLELDGT ENKSKFGANA ILGVSLAVCK
AGAAEKGVPL YRHIADLAGH KDVILPCPAF NVINGGSHAG NKLAMQEFMI LPIGASNFHE
AMRIGAEVYH NLKNVIKAKY GKDATNVGDE GGFAPNILEN NEALELLKTA IEKAGYPDKI
IIGMDVAASE FYKAGKYDLD FKSPDDPARY ITGDQLGDLY KSFIKGYPVQ SIEDPFDQDD
WAAWTKFTAA VDIQVVGDDL TVTNPKRIQQ AVEKKACNCL LLKVNQIGSV TESIKACKLA
QSNGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR SERLAKYNQL MRIEEELGAK
AKFAGKDYRH PKIN
