ID   ENO_CRYPA               Reviewed;         438 AA.
AC   Q6RG04;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, 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;
GN   Name=ENO1;
OS   Cryphonectria parasitica (Chestnut blight fungus) (Endothia parasitica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Diaporthales; Cryphonectriaceae;
OC   Cryphonectria-Endothia species complex; Cryphonectria.
OX   NCBI_TaxID=5116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Kim M.-J., Chung H.-J., Park S.-M., Yang M.-S., Kim D.-H.;
RT   "Cloning and Characterization of Enolase, ENO1, from Cryphonectria
RT   parasitica.";
RL   Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the enolase family. {ECO:0000305}.
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DR   EMBL; AY499570; AAR92205.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6RG04; -.
DR   SMR; Q6RG04; -.
DR   PRIDE; Q6RG04; -.
DR   OMA; EFMIIPV; -.
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   3: Inferred from homology;
KW   Cytoplasm; Glycolysis; Lyase; Magnesium; Metal-binding.
FT   CHAIN           1..438
FT                   /note="Enolase"
FT                   /id="PRO_0000134047"
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;  47360 MW;  9930DF8D795AE6BA CRC64;
     MPISKIHARY VYDSRGNPTV EVDLVTETGL HRAIVPSGAS TGQHEACELR DGDKSKWLGK
     GVLKAVENVN TVLGPELIKA GLDVKDQTAV DEFLIKLDGT ANKTKLGANA ILGVSLAVAK
     AGAAEKGVPL YAHVSDLAGT KKPYVLPVPF QNVLNGGSHA GGRLAFQEFM IVPSAAPSFS
     EGLRWGAETY HQLKSLAKKK YGQSAGNVGD EGGVAPDIQT AEEALELISE AIEKAGYTGK
     MKIAMDVASS EFYKEDVKKY DLDFKNPDSD PSNWLTYEQL AALYADLTKK YPIVSIEDPF
     AEDDWEAWSY FYKTQDIQLV ADDLTVTNPI RIKKAIELKA ANALLLKVNQ IGTLTESIQA
     AKDSYADGWG VMVSHRSGET EDVTIADIVV GIRAGQIKTG APARSERLAK LNQILRIEEE
     LGSNAIYAGE DFRKSVTL