ID   ENO2_MAIZE              Reviewed;         446 AA.
AC   P42895;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Enolase 2;
DE            EC=4.2.1.11;
DE   AltName: Full=2-phospho-D-glycerate hydro-lyase 2;
DE   AltName: Full=2-phosphoglycerate dehydratase 2;
GN   Name=ENO2;
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. B73; TISSUE=Root;
RX   PubMed=9847102; DOI=10.1104/pp.118.4.1285;
RA   Lal S.K., Lee C., Sachs M.M.;
RT   "Differential regulation of enolase during anaerobiosis in maize.";
RL   Plant Physiol. 118:1285-1293(1998).
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; U17973; AAD04187.1; -; mRNA.
DR   PIR; T02221; T02221.
DR   RefSeq; NP_001105371.1; NM_001111901.1.
DR   AlphaFoldDB; P42895; -.
DR   SMR; P42895; -.
DR   STRING; 4577.GRMZM2G048371_P01; -.
DR   Allergome; 9198; Zea m 22.
DR   PaxDb; P42895; -.
DR   PRIDE; P42895; -.
DR   GeneID; 542316; -.
DR   KEGG; zma:542316; -.
DR   MaizeGDB; 30060; -.
DR   eggNOG; KOG2670; Eukaryota.
DR   OrthoDB; 773373at2759; -.
DR   UniPathway; UPA00109; UER00187.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; P42895; 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 2"
FT                   /id="PRO_0000134074"
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;  48163 MW;  DC27708CF92F6850 CRC64;
     MAATIQSVKA RQIFDSRGNP TVEVDVFCSD GTFARAAVPS GASTGVYEAL ELRDGGSYYL
     GKGVSKAVNN VNSVIGPALI GKDPTAQTEI DNFMVQQLDG TKNEWGWCKQ KLGANAILAV
     SLAVCKAGAS IKRIPLYQHI ANLAGNKQLV LPVPAFNVIN GGSHAGNKLA MQEFMILPTG
     AASFKEAMKM GVEVYHHLKS VIKKKYGQDA TNVGDEGGFA PNIQENKEGL ELLKTAIEKA
     GYTGKVVIGM DVAASEFYSD KDQTYDLNFK EENNDGSQKI SGDSLKNVYK SFVSEYPIVS
     IEDPFDQDDW VHYAKMTEEI GEQVQIVGDD LLVTNPTRVA KAIKEKSCNA LLLKVNQIGS
     VTESIEAVKM SKRAGWGVMT SHRSGETEDT FIADLAVGLS TGQIKTGAPC RSERLAKYNQ
     LLRIEEELGA IAVYAGAKFR APVEPY