ID   ENO_MASBA               Reviewed;         439 AA.
AC   Q9U615;
DT   20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
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;
GN   Name=ENOL;
OS   Mastigamoeba balamuthi (Phreatamoeba balamuthi).
OC   Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Mastigamoebidae;
OC   Mastigamoeba.
OX   NCBI_TaxID=108607;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Haennert V., Brinkmann H., Nowitzki U., Lee J.A., Albert M.-A.,
RA   Sensen C.W., Gaasterland T., Muller M., Michels P.A.M., Martin W.;
RT   "Enolase from Trypanosoma brucei, from the amitochondriate protist
RT   Mastigamoeba balamuthi, and from the chloroplast and cytosol of Euglena
RT   gracilis: pieces in the evolutionary puzzle of the eukaryotic glycolytic
RT   pathway.";
RL   Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 30984;
RA   Lee J.A., Moore D.V., Gordon P., Sensen C.W., Gaasterland T., Muller M.;
RT   "cDNA clones (expressed sequence tags) from the free-living amitochondriate
RT   amoeboflagellate, Mastigamoeba balamuthi.";
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; AF205070; AAF13454.1; -; mRNA.
DR   EMBL; AF348478; AAK31161.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9U615; -.
DR   SMR; Q9U615; -.
DR   VEuPathDB; AmoebaDB:MBAL_002915; -.
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..439
FT                   /note="Enolase"
FT                   /id="PRO_0000134087"
FT   ACT_SITE        209
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        349
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         157
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         166
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         244
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         324
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         324
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         376..379
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         400
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   439 AA;  48006 MW;  F2CEDE165BBC31F5 CRC64;
     MSTIKSVFAR EILDSRGNPT VEVDLTTEKG LFRSAVPSGA STGIYEACEL RDGDKSRYLG
     KGVLKAVENV NKILAPKLIG LDVTKQGEID RLMLQIDGTE NKTHLGANAI LGCSMSVCRA
     AAAFRGLPLY RYIAELSGNK SPMLPLPCFN VINGGEHAGN KLAMQEFMIC PTGATSFHEA
     LRMAAETYHN LKLVIKKRYG MDATNVGDEG GFAPNIQANH EGLELIVEAI KQAGYTGKIE
     IGMDVAASSF WDAKESKYDL GFKVPADKKT PDMLVSGEGL IKLYEEWTSK YPIWSIEDPF
     DQDDWATYTR FTELIRNRIQ IVGDDLLVTN PKRIVEARNK KACNALLLKL NQIGSVSEAV
     EACRLAREVN WGVMVSHRSG ETEDAFIADL VVGLGCGQIK TGAPCRSERL AKYNQLLRIE
     EELGANAHYA AKTLSGVGH