ENO1_TOXGO
ID ENO1_TOXGO Reviewed; 444 AA.
AC Q9UAE6;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 97.
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;
OS Toxoplasma gondii.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Toxoplasma.
OX NCBI_TaxID=5811;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RX PubMed=10455162; DOI=10.1074/jbc.274.35.24888;
RA Dzierszinski F., Popescu O., Toursel C., Slomianny C., Yahiaoui B.,
RA Tomavo S.;
RT "The protozoan parasite Toxoplasma gondii expresses two functional plant-
RT like glycolytic enzymes. Implications for evolutionary origin of
RT apicomplexans.";
RL J. Biol. Chem. 274:24888-24895(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=PLK;
RA Kibe M., Tomavo S.;
RT "Toxoplasma gondii enolases ENO1 and ENO2 loci.";
RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP CHARACTERIZATION.
RX PubMed=11399076; DOI=10.1006/jmbi.2001.4730;
RA Dzierszinski F., Mortuaire M., Dendouga N., Popescu O., Tomavo S.;
RT "Differential expression of two plant-like enolases with distinct enzymatic
RT and antigenic properties during stage conversion of the protozoan parasite
RT Toxoplasma gondii.";
RL J. Mol. Biol. 309:1017-1027(2001).
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 -!- DEVELOPMENTAL STAGE: Expressed preferentially in the bradyzoite stage.
CC {ECO:0000269|PubMed:10455162}.
CC -!- MISCELLANEOUS: While ENO1 and ENO2 display similar K(m) values, the
CC pure tachyzoite-specific enzyme (ENO2) has a threefold specific
CC activity at V(max) compared with that of the bradyzoite-specific
CC enolase (ENO1).
CC -!- SIMILARITY: Belongs to the enolase family. {ECO:0000305}.
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DR EMBL; AF051910; AAD51128.1; -; mRNA.
DR EMBL; AY155668; AAP24058.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9UAE6; -.
DR SMR; Q9UAE6; -.
DR PRIDE; Q9UAE6; -.
DR EnsemblProtists; TGME49_268860-t26_1; TGME49_268860-t26_1; TGME49_268860.
DR VEuPathDB; ToxoDB:TGARI_268860; -.
DR VEuPathDB; ToxoDB:TGCAST_268860; -.
DR VEuPathDB; ToxoDB:TGCOUG_268860; -.
DR VEuPathDB; ToxoDB:TGDOM2_268860; -.
DR VEuPathDB; ToxoDB:TGFOU_268860; -.
DR VEuPathDB; ToxoDB:TGGT1_268860; -.
DR VEuPathDB; ToxoDB:TGMAS_268860; -.
DR VEuPathDB; ToxoDB:TGME49_268860; -.
DR VEuPathDB; ToxoDB:TGP89_268860; -.
DR VEuPathDB; ToxoDB:TGPRC2_268860; -.
DR VEuPathDB; ToxoDB:TGRH88_082390; -.
DR VEuPathDB; ToxoDB:TGRUB_268860; -.
DR VEuPathDB; ToxoDB:TGVAND_268860; -.
DR VEuPathDB; ToxoDB:TGVEG_268860; -.
DR OMA; QHLGGAF; -.
DR BRENDA; 4.2.1.11; 6411.
DR SABIO-RK; Q9UAE6; -.
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 1: Evidence at protein level;
KW Cytoplasm; Glycolysis; Lyase; Magnesium.
FT CHAIN 1..444
FT /note="Enolase 1"
FT /id="PRO_0000134093"
FT ACT_SITE 217
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 355
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 165
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 174
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 303
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 330
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 382..385
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 406
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 444 AA; 48341 MW; 667B3558B5B3D768 CRC64;
MVVIKDIVAR EILDSRGNPT IEVDVSTEGG VFRAAVPSGA STGIYEALEL RDKDPKRYLG
KGVLNAVEIV RQEIKPALLG KDPCDQKGID MLMVEQLDGT KNEWGYSKSK LGANAILGVS
IACCRAGAAS KGLPLYKYIA TLAGKTIDKM VMPVPFFNVI NGGEHAGNGL ALQEFLIAPV
GAPNIREAIR YGSETYHHLK NVIKNKYGLD ATNVGDEGGF APNVATAEEA LNLLVEAIKA
AGYEGKIKIA FDAAASEFYK QDEKKYDLDY KCKTKNASKH LTGEKLKEVY EGWLKKYPII
SVEDPFDQDD FASFSAFTKD VGEKTQVIGD DILVTNILRI EKALKDKACN CLLLKVNQIG
SVTEAIEACL LAQKSGWGVQ VSHRSGETED SFIADLVVGL RCGQIKSGSP CRSERLCKYN
QLMRIEESLG ADCVYAGESF RHPK
