ID ENO_PENCI Reviewed; 437 AA. AC Q96X46; DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 06-DEC-2005, sequence version 2. DT 28-NOV-2006, entry version 27. DE Enolase (EC 4.2.1.11) (2-phosphoglycerate dehydratase) (2-phospho-D- DE glycerate hydro-lyase) (Allergen Pen c 22). GN Name=enoA; OS Penicillium citrinum. OC Eukaryota; Fungi; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiales; Trichocomaceae; mitosporic Trichocomaceae; Penicillium. OX NCBI_TaxID=5077; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-21, AND RP ALLERGENICITY. RC STRAIN=52-5; RX MEDLINE=21975100; PubMed=11979043; DOI=10.1159/000053862; RA Lai H.-Y., Tam M.F., Tang R.-B., Chou H., Chang C.-Y., Tsai J.-J., RA Shen H.-D.; RT "cDNA cloning and immunological characterization of a newly identified RT enolase allergen from Penicillium citrinum and Aspergillus RT fumigatus."; RL Int. Arch. Allergy Immunol. 127:181-190(2002). 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. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE. 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; AF254643; AAK51201.1; -; mRNA. DR HSSP; P00924; 4ENL. DR SMR; Q96X46; 2-431. DR InterPro; IPR000941; Enolase. DR Pfam; PF00113; Enolase_C; 1. DR Pfam; PF03952; Enolase_N; 1. DR PRINTS; PR00148; ENOLASE. DR ProDom; PD000902; Enolase; 1. DR TIGRFAMs; TIGR01060; eno; 1. DR PROSITE; PS00164; ENOLASE; 1. KW Allergen; Direct protein sequencing; Glycolysis; Lyase; Magnesium; KW Metal-binding. FT INIT_MET 0 0 FT CHAIN 1 437 Enolase. FT /FTId=PRO_0000134056. FT REGION 373 376 Substrate binding (By similarity). FT ACT_SITE 210 210 Proton donor (By similarity). FT ACT_SITE 346 346 Proton acceptor (By similarity). FT METAL 245 245 Magnesium (By similarity). FT METAL 296 296 Magnesium (By similarity). FT METAL 321 321 Magnesium (By similarity). FT BINDING 158 158 Substrate (By similarity). FT BINDING 167 167 Substrate (By similarity). FT BINDING 296 296 Substrate (By similarity). FT BINDING 321 321 Substrate (By similarity). FT BINDING 397 397 Substrate (By similarity). SQ SEQUENCE 437 AA; 47144 MW; 414A017B47263E3F CRC64; PIAKVHARSV YVSRGNPTVE VDVVTETGLH RAIVPSGAST GQHEAVELRD GDKAKWGGKG VLKAVKNVNE TIGPALIKEN IDVKDQAKVD EFLNKLDGTA NKGNLGANAI LGVSLAIAKA AAAEKGVPLY VHISDLAGTK KPYVLPVPFQ NVLNGGSHAG GRLAFQEFMI VPDTAESFSE GLRQGAEVYQ KLKALAKKKY GQSAGNVGDE GGVAPDIQTA EEALDLITEA IEQAGYTGKI SIAMDVASSE FYKTDAKKYD LDFKNPDSDP TKWLTYEQLA DLYKSLAAKY PIVSIEDPFA EDDWEAWSYF YKTSDFQIVG DDLTVTNPLR IKKAIELKSC NALLLKVNQI GTLTESIQAA KDSYADNWGV MVSHRSGETE DVTIADIAVG LRSGQIKTGA PARSERLAKL NQILRIEEEL GENAIYAGKN FRTSVNL //