ID   ENO_ALNGL               Reviewed;         440 AA.
AC   Q43321;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 91.
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;
OS   Alnus glutinosa (European alder) (Betula alnus var. glutinosa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fagales; Betulaceae; Alnus.
OX   NCBI_TaxID=3517;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Root nodule;
RX   PubMed=8602161; DOI=10.1007/bf02174032;
RA   van Ghelue M., Ribeiro A., Solheim B., Akkermans A.D.L., Bisseling T.,
RA   Pawlowski K.;
RT   "Sucrose synthase and enolase expression in actinorhizal nodules of Alnus
RT   glutinosa: comparison with legume nodules.";
RL   Mol. Gen. Genet. 250:437-446(1996).
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; X92377; CAA63121.1; -; mRNA.
DR   AlphaFoldDB; Q43321; -.
DR   SMR; Q43321; -.
DR   PRIDE; Q43321; -.
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..440
FT                   /note="Enolase"
FT                   /id="PRO_0000134066"
FT   ACT_SITE        216
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        349
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         248
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         297
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         297
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         324
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         324
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         399
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   440 AA;  47597 MW;  EFB3AAC705CE9FA5 CRC64;
     MAEITHIKAR QIFDSRGNPT VEAEVTTANG VVSRAAVPSG ASTGVYEALE LRDGGSDYLG
     KGVLKAVDNV NKIIGPALIG KDATEQTAID IDFMFQQLDG TVNEWGWCKQ KLGANAILAV
     SLAVCKAGAS VKKIPLYKHI ANLAGNPKLV LPVPAFNVIN GGSHAGNKLA MQEFMILPVG
     ASSFKEAMKM GVEVYHHLKA VIKKKYGQDA TNVGDEGGFA PNIQENKEGL ELLKTAIAKA
     GYVVIGMDVA ASEFYEKDKD ITNFKEENND GSQKISADQL KDLYKSFVDE YPIVSIEDPF
     DQDDWEHYSK LTAEIGEKVQ IVGDDLLVTN PKRVEKAIKE KACNALLLKV NQIGSVTESI
     EAVKMSKRAG WGVMAHRSGE TEDTFIADLS VGLATGQIKT GAPCRSERLA KYNQLLRIEE
     ELGSEAVYAG ANFRTPVEPY