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 16-JUN-2009, entry version 50. DE RecName: Full=Enolase 2; DE EC=4.2.1.11; DE AltName: Full=2-phosphoglycerate dehydratase 2; DE AltName: Full=2-phospho-D-glycerate hydro-lyase 2; DE AltName: Allergen=Hev b 9; GN Name=ENO2; OS Hevea brasiliensis (Para rubber tree). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids I; Malpighiales; Euphorbiaceae; Crotonoideae; OC Micrandreae; Hevea. OX NCBI_TaxID=3981; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND ALLERGENICITY. RC TISSUE=Latex; RX MEDLINE=20558236; PubMed=11106410; RX 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 RT latex and molds. Purification, characterization, cloning and RT expression."; RL Eur. J. Biochem. 267:7006-7014(2000). CC -!- CATALYTIC ACTIVITY: 2-phospho-D-glycerate = phosphoenolpyruvate + CC H(2)O. CC -!- COFACTOR: Magnesium. Required for catalysis and for stabilizing CC the dimer (By similarity). CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 4/5. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- ALLERGEN: Causes an allergic reaction in human. Involved in latex CC allergic reactions. CC -!- SIMILARITY: Belongs to the enolase family. 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 HSSP; P56252; 1PDZ. DR BRENDA; 4.2.1.11; 2218. DR GO; GO:0000015; C:phosphopyruvate hydratase complex; IEA:InterPro. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW. DR GO; GO:0004634; F:phosphopyruvate hydratase activity; IEA:EC. DR GO; GO:0006096; P:glycolysis; IEA:UniProtKB-KW. DR InterPro; IPR000941; Enolase. DR PANTHER; PTHR11902; Enolase; 1. DR Pfam; PF00113; Enolase_C; 1. DR Pfam; PF03952; Enolase_N; 1. DR PIRSF; PIRSF001400; Enolase; 1. DR PRINTS; PR00148; ENOLASE. DR ProDom; PD000902; Enolase; 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 Enolase 2. FT /FTId=PRO_0000134070. FT REGION 380 383 Substrate binding (By similarity). FT ACT_SITE 216 216 Proton donor (By similarity). FT ACT_SITE 353 353 Proton acceptor (By similarity). FT METAL 251 251 Magnesium (By similarity). FT METAL 301 301 Magnesium (By similarity). FT METAL 328 328 Magnesium (By similarity). FT BINDING 164 164 Substrate (By similarity). FT BINDING 173 173 Substrate (By similarity). FT BINDING 301 301 Substrate (By similarity). FT BINDING 328 328 Substrate (By similarity). FT BINDING 404 404 Substrate (By similarity). 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 //