ID   ENO_TUBBO               Reviewed;         440 AA.
AC   Q6W3C0;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 65.
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=eno-1;
OS   Tuber borchii (White truffle).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC   Pezizales; Tuberaceae; Tuber.
OX   NCBI_TaxID=42251;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=14732262; DOI=10.1016/j.fgb.2003.10.008;
RA   Polidori E., Saltarelli R., Ceccaroli P., Buffalini M., Pierleoni R.,
RA   Palma F., Bonfante P., Stocchi V.;
RT   "Enolase from the ectomycorrhizal fungus Tuber borchii Vittad.: biochemical
RT   characterization, molecular cloning, and localization.";
RL   Fungal Genet. Biol. 41:157-167(2004).
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;
CC       Note=Mg(2+) is required for catalysis and for stabilizing the dimer.;
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:0000269|PubMed:14732262}.
CC   -!- SIMILARITY: Belongs to the enolase family. {ECO:0000305}.
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DR   EMBL; AY314788; AAQ88397.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6W3C0; -.
DR   SMR; Q6W3C0; -.
DR   PRIDE; Q6W3C0; -.
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; IPR018247; EF_Hand_1_Ca_BS.
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   Cytoplasm; Glycolysis; Lyase; Magnesium; Metal-binding.
FT   CHAIN           1..440
FT                   /note="Enolase"
FT                   /id="PRO_0000134060"
FT   ACT_SITE        211
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        346
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         245
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         321
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         321
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         373..376
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         397
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   440 AA;  47931 MW;  3092929646FE0174 CRC64;
     MITKIHARSV YDSRGNPTVE VDLTTTDTGL HRAIVPSGAS TGQHEAIELR DKDKTKWAGK
     GVLKAVENVN TIIAPALIKE KFDVKDQATI DKFLIDLDGT PNKAKLGANA ILGVSLAVAK
     AGAAAKKVPL YAHVADLAGT KKPFVLPVPF MNVINGGSHA GGRLAFQEFM IVPSEAPSFT
     EAMRQGAEVY QILKTLTKKK YGQSAGNVGD EGGWPDIQTV EEALDLITDA IDKAGYTGQI
     KIAMDVASSE FYKEDAKKYD LDFKNPDSDS SKWLTYQELA DLYKSLAQRY PIVSIEDPFA
     EDDWEAWAHF YKTSDFQIVG DDLTVTNPIR IKRAIDEKSC NALLLKVNQI ATLTESIQAA
     KDSYSAGWGV MVSHRSGETE DVTIADIVVG LRAGQIKTGA PARSERLAKL NQILRIEEEL
     GEQAIYAGTS SEPPHLYIFI