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   03-AUG-2022, entry version 82.
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 = 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 {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}.
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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   PRIDE; Q96X46; -.
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; 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