ID   ENO_EIMTE               Reviewed;         445 AA.
AC   Q967Y8;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 79.
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;
OS   Eimeria tenella (Coccidian parasite).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC   Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX   NCBI_TaxID=5802;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=PAPt38;
RA   Labbe M., Pery P.;
RT   "Molecular cloning of a cDNA encoding an enolase of Eimeria tenella.";
RL   Submitted (FEB-2001) 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; AF353515; AAK38886.1; -; mRNA.
DR   AlphaFoldDB; Q967Y8; -.
DR   SMR; Q967Y8; -.
DR   PRIDE; Q967Y8; -.
DR   VEuPathDB; ToxoDB:ETH2_1011400; -.
DR   VEuPathDB; ToxoDB:ETH_00024910; -.
DR   BRENDA; 4.2.1.11; 2046.
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   2: Evidence at transcript level;
KW   Cytoplasm; Glycolysis; Lyase; Magnesium; Metal-binding.
FT   CHAIN           1..445
FT                   /note="Enolase"
FT                   /id="PRO_0000134088"
FT   ACT_SITE        217
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        355
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         165
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         174
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         252
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         303
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         303
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         330
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         330
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         382..385
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         406
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   445 AA;  47975 MW;  9FA3B7465B860E77 CRC64;
     MVAIVEVKAR EILDSRGNPT VEVDLKTEQG CFRAAVPSGA STGIYEALEL RDGDKTRYNG
     KGVLKAVENV NKVLAPALVG KDCREQAALD RLMVEELDGS KNEWGWSKSV LGANAILAVS
     MALCRAGAAA KGIPLYKYVA QLAGHEAPEF VLPVPCFNVL NGGKHAGNSL AMQEFMVAPV
     GARSFGEALR MGAEVYQALQ RLLKAKFGLA ATNVGDEGGF APDIKDPREA LGLLVEAIRA
     AGHEGKVKIM ADVAASEFYS KEAKSYDLDF KSPAADAHRL LTGDQLKDLF KEWSEEFPIV
     SIEDPFDQDD FSSYAALTAE IGSKVQVVGD DLLVTNPARI RKALQHKACN ALLLKVNQIG
     SITEAIEACK LAQASGWGVM VSHRSGETED SFIADLVVGL RTGQIKTGAP CRSERLCKYN
     QLLRIEEQLQ GRCTYAGENF RNPSN