ENO2_HEVBR
ID ENO2_HEVBR Reviewed; 445 AA.
AC Q9LEI9;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Enolase 2;
DE EC=4.2.1.11;
DE AltName: Full=2-phospho-D-glycerate hydro-lyase 2;
DE AltName: Full=2-phosphoglycerate dehydratase 2;
DE AltName: Allergen=Hev b 9;
GN Name=ENO2;
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}.
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DR EMBL; AJ132581; CAC00533.1; -; mRNA.
DR AlphaFoldDB; Q9LEI9; -.
DR SMR; Q9LEI9; -.
DR Allergome; 3317; Hev b 9.0101.
DR Allergome; 404; Hev b 9.
DR PRIDE; Q9LEI9; -.
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 2"
FT /id="PRO_0000134070"
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; 47914 MW; C5B42954F0E83EC8 CRC64;
MAITIVSVRA RQIFDSRGNP TVEADVKLSD GYLARAAVPR GASTGIYEAL ELRDGGSDYL
GKGVSKAVEN VNIIIGPALV GKDPTDQVGI DNFMVQQLDG TVNEWGWCKQ KLGANAILAV
SLAVCKAGAH VKGIPLYKHV ANLAGNKNLV LPVPAFNVIN GGSHAGNKLA MQEFMILPVG
ASSFKEAMKM GAEVYHHLKS VIKKKYGQDA TNVGDEGGFA PNIQENKEGL ELLKTAIAKA
GYTGKVVIGM DVAASEFYGS DKTYDLNFKE ENNNGSQKIS GDVLKDLYKS FVTEYPIVSI
EDPFDQDDWE HYAKLTSEIG VKVQIVGDDL LVTNPKRVEK AIKEKACNAL LLKVNQIGSV
TESIEAVKMS KRAGWGVMAS HRSGETEDTF IADLSVGLAT GQIKTGAPCR SERLAKYNQL
LRIEEELGAE AVYAGANFRT PVEPY
