ID   ENO1_MAIZE              Reviewed;         446 AA.
AC   P26301;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Enolase 1;
DE            EC=4.2.1.11;
DE   AltName: Full=2-phospho-D-glycerate hydro-lyase 1;
DE   AltName: Full=2-phosphoglycerate dehydratase 1;
GN   Name=ENO1; Synonyms=PGH1;
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Berkeley Fast; TISSUE=Root;
RX   PubMed=1859865; DOI=10.1007/bf00015071;
RA   Lal S.K., Johnson S., Conway T., Kelley P.M.;
RT   "Characterization of a maize cDNA that complements an enolase-deficient
RT   mutant of Escherichia coli.";
RL   Plant Mol. Biol. 16:787-795(1991).
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.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the enolase family. {ECO:0000305}.
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DR   EMBL; X55981; CAA39454.1; -; mRNA.
DR   PIR; S16257; S16257.
DR   RefSeq; NP_001105896.1; NM_001112426.1.
DR   AlphaFoldDB; P26301; -.
DR   SMR; P26301; -.
DR   STRING; 4577.GRMZM2G064302_P01; -.
DR   PaxDb; P26301; -.
DR   PRIDE; P26301; -.
DR   ProMEX; P26301; -.
DR   GeneID; 732811; -.
DR   KEGG; zma:732811; -.
DR   MaizeGDB; 30060; -.
DR   eggNOG; KOG2670; Eukaryota.
DR   OrthoDB; 773373at2759; -.
DR   UniPathway; UPA00109; UER00187.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; P26301; baseline and differential.
DR   GO; GO:0000015; C:phosphopyruvate hydratase complex; IBA:GO_Central.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004634; F:phosphopyruvate hydratase activity; IBA:GO_Central.
DR   GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
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; Reference proteome.
FT   CHAIN           1..446
FT                   /note="Enolase 1"
FT                   /id="PRO_0000134073"
FT   ACT_SITE        216
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        354
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         302
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         302
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         329
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         329
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         381..384
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         405
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   446 AA;  48064 MW;  6266C48914F35198 CRC64;
     MAVTITWVKA RQIFDSRGNP TVEVDVGLSD GSYARGAVPS GASTGIYEAL ELRDGGSDYL
     GKGVLKAVSN VNNIIGPAIV GKDPTEQVEI DNFMVQQLDG TSNEWGWCKQ KLGANAILAV
     SLAVCKAGAM VKKIPLYQHI ANLAGNKTLV LPVPAFNVIN GGSHAGNKLA MQEFMILPTG
     ASSFKEAMKM GVEVYHNLKS IIKKKYGQDA TNVGDEGGFA PNIQENKEGL ELLKAAIEKA
     GYTGKVVIGM DVAASEFFGE KDKTYDLNFK EENNDGSNKI SGDSLKDLYK SFVSEYPIES
     IEDPFDQDDW STYAKLTDEI GQKVQIVGDD LLVTNPTRVA KAINEKTCNA LLLKVNQIGS
     VTESIEAVRM SKRAGWGVMA SHRSGETEDT FIADLSVGLS TGQIKTGAPC RSERLAKYNQ
     LLRIEEELGD AAVYAGAKFR APVEPY