ID   ENO_RHOMI               Reviewed;         439 AA.
AC   Q870B9;
DT   26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 76.
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=Rho m 1;
GN   Name=ENO;
OS   Rhodotorula mucilaginosa (Yeast) (Rhodotorula rubra).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX   NCBI_TaxID=5537;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND ALLERGEN.
RX   PubMed=12432231; DOI=10.1159/000067279;
RA   Chang C.-Y., Chou H., Tam M.F., Tang R.B., Lai H.-Y., Shen H.-D.;
RT   "Characterization of enolase allergen from Rhodotorula mucilaginosa.";
RL   J. Biomed. Sci. 9:645-655(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:12432231}.
CC   -!- SIMILARITY: Belongs to the enolase family. {ECO:0000305}.
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DR   EMBL; AF382946; AAP30720.1; -; mRNA.
DR   AlphaFoldDB; Q870B9; -.
DR   SMR; Q870B9; -.
DR   Allergome; 3465; Rho m 1.0101.
DR   Allergome; 613; Rho m 1.
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; Glycolysis; Lyase; Magnesium; Metal-binding.
FT   CHAIN           1..439
FT                   /note="Enolase"
FT                   /id="PRO_0000134057"
FT   ACT_SITE        212
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        348
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         160
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         169
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         247
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         296
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         296
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         323
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         323
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         375..378
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         399
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   439 AA;  47140 MW;  2C3DD18F63D33F34 CRC64;
     MAISKIHSRY VYDSRGNPTV EVELTTEKGT FRSIVPSGAS TGVHEALELR DGDKSKWLGK
     GVLKAVANVN DTIAPALIEA NIDVADQAKI DEFLLKLDGT PNKAKLGANA ILGVSLAAAK
     AGAAQKDVPL YKHIADISKA KEGKFVLPVP FQNVLNGGSH AGGDLAFQEF MIVPSGAPSF
     SEGLRIGSEV YHHLKSLTKK KYGQSAGNVG DEGGVAPDIK TAKEALDLIV SAIEAAGYTG
     QVDIAMDVAS SEFYKDGLYD LDFKNPNSDK SKWITGPQLA ELYEQLLNEY PIVSIEDPFA
     EDDWEAWSHF FSKVEGKTQI VGDDLTVTNP IRIKKAIETK AADALLLKVN QIGTLTESIQ
     AANDSYAAGW GVMVSHRSGE TEDTFIADLS VGIRSGQTKT GAPARSERLA KLNQILRIEE
     ELGDKAIYAG KDFHKAHSL