ENO1_HEVBR
ID ENO1_HEVBR Reviewed; 445 AA.
AC Q9LEJ0;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Enolase 1;
DE EC=4.2.1.11;
DE AltName: Full=2-phospho-D-glycerate hydro-lyase 1;
DE AltName: Full=2-phosphoglycerate dehydratase 1;
DE AltName: Allergen=Hev b 9;
GN Name=ENO1;
OS Hevea brasiliensis (Para rubber tree) (Siphonia brasiliensis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Micrandreae;
OC Hevea.
OX NCBI_TaxID=3981;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND ALLERGEN.
RC TISSUE=Latex;
RX PubMed=11106410; DOI=10.1046/j.1432-1327.2000.01801.x;
RA Wagner S., Breiteneder H., Simon-Nobbe B., Susani M., Krebitz M.,
RA Niggemann B., Brehler R., Scheiner O., Hoffmann-Sommergruber K.;
RT "Hev b 9, an enolase and a new cross-reactive allergen from hevea latex and
RT molds. Purification, characterization, cloning and expression.";
RL Eur. J. Biochem. 267:7006-7014(2000).
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Mg(2+) is required for catalysis and for stabilizing the dimer.
CC {ECO:0000250};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 4/5.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALLERGEN: Causes an allergic reaction in human. Involved in latex
CC allergic reactions. {ECO:0000269|PubMed:11106410}.
CC -!- SIMILARITY: Belongs to the enolase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ132580; CAC00532.1; -; mRNA.
DR AlphaFoldDB; Q9LEJ0; -.
DR SMR; Q9LEJ0; -.
DR Allergome; 3317; Hev b 9.0101.
DR Allergome; 404; Hev b 9.
DR PRIDE; Q9LEJ0; -.
DR BioCyc; MetaCyc:MON-12858; -.
DR BRENDA; 4.2.1.11; 2665.
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; Glycolysis; Lyase; Magnesium; Metal-binding.
FT CHAIN 1..445
FT /note="Enolase 1"
FT /id="PRO_0000134069"
FT ACT_SITE 216
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 353
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 173
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 251
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 301
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 301
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 328
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 328
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 380..383
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 404
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 445 AA; 47830 MW; 238883FB249F5544 CRC64;
MAITIVSVRA RQIFDSRGNP TVEADVKLSD GYLARAAVPS GASTGIYEAL ELRDGGSDYL
GKGVSKAVEN VNIIIGPALV GKDPTDQVGI DNFMVQQLDG TVNEWGWCKQ KLGANAILAV
SLAVCKAGAH VKGIPLYEHI ANLAGNKNLV LPVPAFNVIN GGSHAGNKLA MQEFMILPVG
ASSFKEAMKM GAEVYHHLKS VIKKKYGQDA TNVGDEGGFA PNIQENKEGL ELLKTAIAKA
GYTGKVVIGM DVAASEFYGS DQTYDLNFKE ENNNGSQKIS GEALKDLYKS FVAEYPIVSI
EDPFDQDDWA HYAKLTSEIG EKVQIVGDDL LVTNPKRVEK AIKEKACNAL LLKVNQIGSV
TESIEAVKMS KRAGWGVMAS HRSGETEDTF IADLSVGLAT GQIKTGAPCR SERLAKYNQL
LRIEEELGSE AVYAGANFRK PVEPY
