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 27-NOV-2024, entry version 86. DE RecName: Full=Enolase; DE EC=4.2.1.11; DE AltName: Full=2-phospho-D-glycerate hydro-lyase; DE AltName: Full=2-phosphoglycerate dehydratase; DE AltName: Allergen=Pen c 22; GN Name=enoA; OS Penicillium citrinum. OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium. OX NCBI_TaxID=5077; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-22, AND ALLERGEN. RC STRAIN=52-5; RX 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 fumigatus."; RL Int. Arch. Allergy Immunol. 127:181-190(2002). CC -!- CATALYTIC ACTIVITY: CC Reaction=(2R)-2-phosphoglycerate = phosphoenolpyruvate + H2O; 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 {ECO:0000250}. CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE. CC {ECO:0000269|PubMed:11979043}. 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; AF254643; AAK51201.1; -; mRNA. DR AlphaFoldDB; Q96X46; -. DR SMR; Q96X46; -. DR Allergome; 3403; Pen c 22.0101. DR Allergome; 522; Pen c 22. 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 FunFam; 3.30.390.10:FF:000001; Enolase; 1. DR FunFam; 3.20.20.120:FF:000002; Enolase 1; 1. DR Gene3D; 3.20.20.120; Enolase-like C-terminal domain; 1. DR Gene3D; 3.30.390.10; Enolase-like, N-terminal domain; 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 NCBIfam; TIGR01060; eno; 1. DR PANTHER; PTHR11902; ENOLASE; 1. DR PANTHER; PTHR11902:SF1; ENOLASE; 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 SFLD; SFLDG00178; enolase; 1. DR SMART; SM01192; Enolase_C; 1. DR SMART; SM01193; Enolase_N; 1. DR SUPFAM; SSF51604; Enolase C-terminal domain-like; 1. DR SUPFAM; SSF54826; Enolase N-terminal domain-like; 1. DR PROSITE; PS00164; ENOLASE; 1. PE 1: Evidence at protein level; KW Allergen; Cytoplasm; Direct protein sequencing; Glycolysis; Lyase; KW Magnesium; Metal-binding. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:11979043" FT CHAIN 2..438 FT /note="Enolase" FT /id="PRO_0000134056" FT ACT_SITE 211 FT /note="Proton donor" FT /evidence="ECO:0000250" FT ACT_SITE 347 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT BINDING 159 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 168 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 246 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 297 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 297 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 322 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 322 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 374..377 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 398 FT /ligand="substrate" FT /evidence="ECO:0000250" 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 //