ENO_SOLLC
ID ENO_SOLLC Reviewed; 444 AA.
AC P26300;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Enolase {ECO:0000303|PubMed:1841726};
DE EC=4.2.1.11 {ECO:0000269|PubMed:1841726};
DE AltName: Full=2-phospho-D-glycerate hydro-lyase;
DE AltName: Full=2-phosphoglycerate dehydratase;
GN Name=PGH1;
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=cv. Supersonic;
RX PubMed=1841726; DOI=10.1105/tpc.3.7.719;
RA van der Straeten D., Rodrigues-Pousada R.A., Goodman H.M., van Montagu M.;
RT "Plant enolase: gene structure, expression, and evolution.";
RL Plant Cell 3:719-735(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 Evidence={ECO:0000269|PubMed:1841726};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10165;
CC Evidence={ECO:0000269|PubMed:1841726};
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. {ECO:0000269|PubMed:1841726}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the enolase family. {ECO:0000305}.
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DR EMBL; X58108; CAA41115.1; -; mRNA.
DR PIR; JQ1185; JQ1185.
DR RefSeq; NP_001234080.1; NM_001247151.2.
DR AlphaFoldDB; P26300; -.
DR SMR; P26300; -.
DR STRING; 4081.Solyc09g009020.2.1; -.
DR PaxDb; P26300; -.
DR PRIDE; P26300; -.
DR EnsemblPlants; Solyc09g009020.3.1; Solyc09g009020.3.1; Solyc09g009020.3.
DR GeneID; 544068; -.
DR Gramene; Solyc09g009020.3.1; Solyc09g009020.3.1; Solyc09g009020.3.
DR KEGG; sly:544068; -.
DR eggNOG; KOG2670; Eukaryota.
DR HOGENOM; CLU_031223_0_0_1; -.
DR InParanoid; P26300; -.
DR OMA; KHADNGI; -.
DR OrthoDB; 773373at2759; -.
DR PhylomeDB; P26300; -.
DR UniPathway; UPA00109; UER00187.
DR Proteomes; UP000004994; Chromosome 9.
DR ExpressionAtlas; P26300; 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 1: Evidence at protein level;
KW Cytoplasm; Glycolysis; Lyase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..444
FT /note="Enolase"
FT /id="PRO_0000134072"
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"
SQ SEQUENCE 444 AA; 47798 MW; 73C384181ED620A0 CRC64;
MATIKSIKAR QIFDSRGNPT VEVDVHISNG VFARAAVPSG ASTGIYEALE LRDGGSDYLG
KGVSKAVNNV NSIIGPALVG KDPTDQTGLD NFMVHQLDGT QNEWGWCKEK LGANAILAVS
LAVCKAGAAV RNVPLYKHIA DLAGNKKLVL PVPAFNVING GSHAGNKLAM QEFMILPVGA
ANFKEAMKMG CEVYHHLKAV IKKKYGQDAT NVGDEGGFAP NIQENKEGLE LLKTAIEKAG
YTGKVVIGMD VAASEFYGKD KSYDLNFKEE SNDGSQKISG DQLKDLYKSF VSEYPIVSIE
DPFDQDDWET YAKLTAEIGE QVQIVGDDLL VTNPKRVAKA IAEKTCNALL LKVNQIGSVT
ESIEAVKMSK KAGWGVMTSH RSGETEDTFI ADLAVGLSTG QIKTGAPCRS ERLAKYNQLL
RIEEELGSEA VYAGASFRKP VEPY
