ID   ENO_MESCR               Reviewed;         444 AA.
AC   Q43130; Q42907;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 93.
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=PGH1; Synonyms=PGH1B;
OS   Mesembryanthemum crystallinum (Common ice plant) (Cryophytum crystallinum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Aizoaceae; Mesembryanthemum;
OC   Mesembryanthemum subgen. Cryophytum.
OX   NCBI_TaxID=3544;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7630941; DOI=10.1104/pp.108.3.1185;
RA   Forsthoefel N.R., Cushman M.A., Cushman J.C.;
RT   "Posttranscriptional and posttranslational control of enolase expression in
RT   the facultative Crassulacean acid metabolism plant Mesembryanthemum
RT   crystallinum L.";
RL   Plant Physiol. 108:1185-1195(1995).
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; S79242; AAB34986.1; -; mRNA.
DR   EMBL; U09194; AAA21277.1; -; mRNA.
DR   PIR; T12341; T12341.
DR   AlphaFoldDB; Q43130; -.
DR   SMR; Q43130; -.
DR   PRIDE; Q43130; -.
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..444
FT                   /note="Enolase"
FT                   /id="PRO_0000134075"
FT   ACT_SITE        215
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        352
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         163
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         172
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         250
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         300
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         300
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         327
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         327
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         379..382
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         403
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   VARIANT         345
FT                   /note="P -> S"
SQ   SEQUENCE   444 AA;  48349 MW;  044E21DF1E5BA166 CRC64;
     MVTIKCVKAR QIYDSRGNPT VEADIHLDDG TYARAAVPSG ASTGVYEALE LRDGGKDYMG
     KGVYKAVKNV NEIIGPALVG KDPTQQTAID NFMVQQLDGT VNEWGWCKQK LGANAILAVS
     LAVCKAGAQV KKIPLYQHIA EIAGNKNMVL PVPAFNVING GSHAGNKLAM QEFMILPTGA
     SSFKEAMKMG SEVYHNLKSV IKKKYGQDAT NVGDEGGFAP NIQENKEGLE LLKTAIEKAG
     YTGKVVIGMD VAASEFYKED KSYDLNFKEE NNDGSQRISG EALKDLYKSF VAEYPIVSIE
     DPFDQDDWEH YAKMTAECGE KVQIVGDDLL VTNPKRVKKA IDENPCNALL LKVNQIGSVT
     ESIEAVKMSK KAGWGVMASH RSGETEDTFI ADLSVGLSTG QIKTGAPCRS ERLAKYNQLL
     RIEEELGDKA VYAGANFRRP VEPY