ID   ENO_CHLRE               Reviewed;         372 AA.
AC   P31683;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 116.
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   Flags: Fragment;
GN   Name=ENO;
OS   Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX   NCBI_TaxID=3055;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=137c / CC-125;
RA   Dumont F., Joris B., Gumusboga A., Bruyninx M., Loppes R.;
RT   "Isolation and characterization of cDNA sequences controlled by inorganic
RT   phosphate in Chlamydomonas reinhardtii.";
RL   Plant Sci. 89:55-67(1993).
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.
CC   -!- SIMILARITY: Belongs to the enolase family. {ECO:0000305}.
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DR   EMBL; X66412; CAA47043.1; -; mRNA.
DR   PIR; S24996; S24996.
DR   AlphaFoldDB; P31683; -.
DR   SMR; P31683; -.
DR   STRING; 3055.EDO96709; -.
DR   ProMEX; P31683; -.
DR   EnsemblPlants; PNW75116; PNW75116; CHLRE_12g513200v5.
DR   Gramene; PNW75116; PNW75116; CHLRE_12g513200v5.
DR   eggNOG; KOG2670; Eukaryota.
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   PRINTS; PR00148; ENOLASE.
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..372
FT                   /note="Enolase"
FT                   /id="PRO_0000134068"
FT   ACT_SITE        147
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        282
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         95
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         104
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         182
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         232
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         232
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         257
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         257
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         309..312
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         333
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   372 AA;  40110 MW;  D7A04BA9D25B1058 CRC64;
     VTKAVENINA IIAPALKGMD PVKQAEIDQK MKDLDGTDNK GKLGANAILA VSMAVCKAGA
     AEKGVPLYKH IADLAGNSKL ILPVPSFNII NGGSHAGNAL AMQEFMILPV GASSFSEAMR
     MGCEVYHALK GLIKAKYGQD ACNVGDEGGF APNIGSNDEG LNLVNEAIEK AGYTGKVKIG
     MDVASSEFYT EDGMYDLDFK NQPNDGSQKK TKEQMLELYN EFCKKYPVIS IEDPFEQDDW
     EPCAKLTTEN ICQVVGDDIL VTNPVRVKKA IDAKAVNALL LKVNQIGTIT ESIEAVRMAK
     EAGWGVMTSH RSGETEDSFI ADLAVGLASG QIKTGAPCRS ERNAKYNQLL RIEEELGENA
     VYAGESWRHI GW