ID   ENO_RICCO               Reviewed;         445 AA.
AC   P42896;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 98.
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;
OS   Ricinus communis (Castor bean).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC   Ricinus.
OX   NCBI_TaxID=3988;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Baker 296; TISSUE=Endosperm;
RX   PubMed=8029364; DOI=10.1104/pp.105.1.455;
RA   Blakeley S.D., Dekroon C., Cole K.P., Kraml M., Dennis D.T.;
RT   "Isolation of a full-length cDNA encoding cytosolic enolase from Ricinus
RT   communis.";
RL   Plant Physiol. 105:455-456(1994).
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.
CC   -!- SIMILARITY: Belongs to the enolase family. {ECO:0000305}.
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DR   EMBL; Z28386; CAA82232.1; -; mRNA.
DR   PIR; S39203; S39203.
DR   RefSeq; NP_001310701.1; NM_001323772.1.
DR   AlphaFoldDB; P42896; -.
DR   SMR; P42896; -.
DR   STRING; 3988.XP_002528580.1; -.
DR   PRIDE; P42896; -.
DR   GeneID; 8288376; -.
DR   KEGG; rcu:8288376; -.
DR   eggNOG; KOG2670; Eukaryota.
DR   SABIO-RK; P42896; -.
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_0000134078"
FT   ACT_SITE        216
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        353
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         164
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         173
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         251
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         301
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         301
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         328
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         328
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         380..383
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         404
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   445 AA;  47912 MW;  A88EFE3A90CAE572 CRC64;
     MAITIVSVRA RQIFDSRGNP TVEADIKLSD GHLARAAVPS GASTGIYEAL ELRDGGSDYL
     GKGVSKAVEN VNSIIGPALI GKDPTEQTAL DNFMVQELDG TVNEWGWCKQ KLGANAILAV
     SLALCKAGAH VKGIPLYKHI ANLAGNKNLV LPVPAFNVIN GGSHAGNKLA MQEFMILPVG
     ASSFKEAMKM GAEVYHHLKS VIKKKYGQDA TNVGDEGGFA PNIQENKEGL ELLKTAIAKA
     GYTGKVVIGM DVAASEFYGS DKTYDLNFKE ENNDGSQKIS GEALKDLYKS FASEYPIVSI
     EDPFDQDDWE HYSKLTSEIG EKVQIVGDDL LVTNPKRVEK AIQEKACNAL LLKVNQIGSV
     TESIEAVRMS KRAGWGVMAS HRSGETEDTF IADLSVGLAT GQIKTGAPCR SERLAKYNQL
     LRIEEELGAE AVYAGAKFRT PVEPY