ENO2_TOXGO
ID ENO2_TOXGO Reviewed; 444 AA.
AC Q9BPL7;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 82.
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 Toxoplasma gondii.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Toxoplasma.
OX NCBI_TaxID=5811;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, AND DEVELOPMENTAL STAGE.
RC STRAIN=76K;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE.
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.
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 tachyzoite stage.
CC {ECO:0000269|PubMed:11399076}.
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; AF123457; AAG60329.1; -; mRNA.
DR EMBL; AY155668; AAP24057.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9BPL7; -.
DR SMR; Q9BPL7; -.
DR EnsemblProtists; TGME49_268850-t26_1; TGME49_268850-t26_1; TGME49_268850.
DR VEuPathDB; ToxoDB:TGARI_268850; -.
DR VEuPathDB; ToxoDB:TGCAST_268850; -.
DR VEuPathDB; ToxoDB:TGCOUG_268850; -.
DR VEuPathDB; ToxoDB:TGDOM2_268850; -.
DR VEuPathDB; ToxoDB:TGFOU_268850; -.
DR VEuPathDB; ToxoDB:TGGT1_268850; -.
DR VEuPathDB; ToxoDB:TGMAS_268850; -.
DR VEuPathDB; ToxoDB:TGME49_268850; -.
DR VEuPathDB; ToxoDB:TGP89_268850; -.
DR VEuPathDB; ToxoDB:TGPRC2_268850; -.
DR VEuPathDB; ToxoDB:TGRH88_082400; -.
DR VEuPathDB; ToxoDB:TGRUB_268850; -.
DR VEuPathDB; ToxoDB:TGVAND_268850; -.
DR VEuPathDB; ToxoDB:TGVEG_268850; -.
DR BRENDA; 4.2.1.11; 6411.
DR SABIO-RK; Q9BPL7; -.
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; Metal-binding.
FT CHAIN 1..444
FT /note="Enolase 2"
FT /id="PRO_0000134094"
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 252
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 303
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 303
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 330
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
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; 48290 MW; 4029B1EA9024D1A1 CRC64;
MVAIKDITAR QILDSRGNPT VEVDLLTDGG CFRAAVPSGA STGIYEALEL RDKDQTKFMG
KGVMKAVENI HKIIKPALIG KDPCDQKGID KLMVEELDGT KNEWGWCKSK LGANAILAVS
MACCRAGAAA KGMPLYKYIA TLAGNPTDKM VMPVPFFNVI NGGSHAGNKV AMQEFMIAPV
GASTIQEAIQ IGAEVYQHLK VVIKKKYGLD ATNVGDEGGF APNISGATEA LDLLMEAIKV
SGHEGKVKIA ADVAASEFFL QDDKVYDLDF KTPNNDKSQR KTGEELRNLY KDLCQKYPFV
SIEDPFDQDD FHSYAQLTNE VGEKVQIVGD DLLVTNPTRI EKAVQEKACN GLLLKVNQIG
TVSESIEACQ LAQKNKWGVM VSHRSGETED SFIADLVVGL RTGQIKTGAP CRSERLCKYN
QLMRIEESLG SDCQYAGAGF RHPN
