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 07-APR-2021, entry version 90. 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}. 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; AJ132581; CAC00533.1; -; mRNA. 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 REGION 380..383 FT /note="Substrate binding" FT /evidence="ECO:0000250" 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 METAL 251 FT /note="Magnesium" FT /evidence="ECO:0000250" FT METAL 301 FT /note="Magnesium" FT /evidence="ECO:0000250" FT METAL 328 FT /note="Magnesium" FT /evidence="ECO:0000250" FT BINDING 164 FT /note="Substrate" FT /evidence="ECO:0000250" FT BINDING 173 FT /note="Substrate" FT /evidence="ECO:0000250" FT BINDING 301 FT /note="Substrate" FT /evidence="ECO:0000250" FT BINDING 328 FT /note="Substrate" FT /evidence="ECO:0000250" FT BINDING 404 FT /note="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 //