ID ENO_PENCI Reviewed; 438 AA. AC Q96X46; DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 12-JUN-2007, entry version 31. 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 2-22, 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 4/5. 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; 3-432. DR InterPro; IPR000941; Enolase. DR PANTHER; PTHR11902; Enolase; 1. 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 1 1 Removed. FT CHAIN 2 438 Enolase. FT /FTId=PRO_0000134056. FT REGION 374 377 Substrate binding (By similarity). FT ACT_SITE 211 211 Proton donor (By similarity). FT ACT_SITE 347 347 Proton acceptor (By similarity). FT METAL 246 246 Magnesium (By similarity). FT METAL 297 297 Magnesium (By similarity). FT METAL 322 322 Magnesium (By similarity). FT BINDING 159 159 Substrate (By similarity). FT BINDING 168 168 Substrate (By similarity). FT BINDING 297 297 Substrate (By similarity). FT BINDING 322 322 Substrate (By similarity). FT BINDING 398 398 Substrate (By similarity). SQ SEQUENCE 438 AA; 47275 MW; 48EA499055C9DE84 CRC64; MPIAKVHARS VYVSRGNPTV EVDVVTETGL HRAIVPSGAS TGQHEAVELR DGDKAKWGGK GVLKAVKNVN ETIGPALIKE NIDVKDQAKV DEFLNKLDGT ANKGNLGANA ILGVSLAIAK AAAAEKGVPL YVHISDLAGT KKPYVLPVPF QNVLNGGSHA GGRLAFQEFM IVPDTAESFS EGLRQGAEVY QKLKALAKKK YGQSAGNVGD EGGVAPDIQT AEEALDLITE AIEQAGYTGK ISIAMDVASS EFYKTDAKKY DLDFKNPDSD PTKWLTYEQL ADLYKSLAAK YPIVSIEDPF AEDDWEAWSY FYKTSDFQIV GDDLTVTNPL RIKKAIELKS CNALLLKVNQ IGTLTESIQA AKDSYADNWG VMVSHRSGET EDVTIADIAV GLRSGQIKTG APARSERLAK LNQILRIEEE LGENAIYAGK NFRTSVNL //