ENO_PLAFG
ID ENO_PLAFG Reviewed; 446 AA.
AC Q9UAL5;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Enolase {ECO:0000303|Ref.1};
DE EC=4.2.1.11 {ECO:0000250|UniProtKB:W7JLR6};
DE AltName: Full=2-phospho-D-glycerate hydro-lyase {ECO:0000305};
DE AltName: Full=2-phosphoglycerate dehydratase {ECO:0000305};
GN Name=ENO {ECO:0000250|UniProtKB:Q8IJN7};
OS Plasmodium falciparum (isolate FCR-3 / Gambia).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=5838;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Kawazu S., Hatabu T., Mizuno Y., Miyamoto K., Suzuki M., Kano S.;
RT "Plasmodium falciparum enolase.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Glycolytic enzyme that catalyzes the conversion of 2-
CC phosphoglycerate to phosphoenolpyruvate (By similarity). In addition to
CC glycolysis, involved in various processes such as parasite development
CC and invasion (By similarity). Plays an essential role during ookinete
CC invasion of the mosquito vector midgut by mediating the interaction of
CC the ookinete with the midgut epithelium and, further, by binding to
CC mammalian host plasminogen in the blood meal, whose conversion to
CC active plasmin promotes the invasion process (By similarity).
CC {ECO:0000250|UniProtKB:W7JLR6}.
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:0000250|UniProtKB:W7JLR6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10165;
CC Evidence={ECO:0000250|UniProtKB:W7JLR6};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10166;
CC Evidence={ECO:0000250|UniProtKB:W7JLR6};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q8IJN7};
CC Note=Binds 2 Mg(2+) ions per subunit (By similarity). Mg(2+) is
CC required for catalysis and for stabilizing the dimer (By similarity).
CC Unlike for mammalian and yeast enolases, Mg(2+) is dispensable to form
CC an active closed conformation (By similarity). Inhibited by high levels
CC of Mg(2+) (By similarity). {ECO:0000250|UniProtKB:Q8IJN7,
CC ECO:0000250|UniProtKB:W7JLR6};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 4/5. {ECO:0000250|UniProtKB:Q8IJN7}.
CC -!- SUBUNIT: Homodimer (By similarity). Forms a complex at least composed
CC of DegP, ENO and HSP70 (By similarity). Interacts with G-actin (By
CC similarity). Interacts (via the DKSLVK motif) with mammalian host
CC PLG/plasminogen (present in the mosquito blood meal); the interaction
CC occurs at the ookinete cell surface and is required for ookinete
CC invasion of the mosquito midgut (By similarity). Interacts with
CC A.gambiae EBP; depending on the Plasmodium species, the interaction is
CC either involved in ookinete invasion of the mosquito midgut (P.berghei)
CC or is dispensable (P.falciparum) (By similarity).
CC {ECO:0000250|UniProtKB:Q8IJN7, ECO:0000250|UniProtKB:W7JLR6}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8IJN7}. Nucleus
CC {ECO:0000250|UniProtKB:Q8IJN7}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:W7JLR6}. Cell surface
CC {ECO:0000250|UniProtKB:Q8IJN7}. Cell membrane
CC {ECO:0000250|UniProtKB:Q7RA60}; Peripheral membrane protein
CC {ECO:0000305}; Cytoplasmic side {ECO:0000250|UniProtKB:Q7RA60}. Vacuole
CC {ECO:0000250|UniProtKB:Q8IJN7}. Note=Partially localizes to the nucleus
CC in rings and trophozoites. Localization to the nucleus and food vacuole
CC is higher in early and mid-stage trophozoites compared to the late-
CC stage trophozoites and schizonts (By similarity). In the nucleus,
CC localizes to heterochromatin region (By similarity). In rings, nuclear
CC localization is dependent on the actin cytoskeleton (By similarity).
CC Localizes to the cell surface of merozoites (By similarity). In
CC gametocytes, predominantly localizes to the actin cytoskeleton (By
CC similarity). In the trophozoite food vacuole, colocalizes with
CC hemozoin, a product of heme detoxification (By similarity). In
CC sporozoites, localizes to punctate structures beneath the cell membrane
CC (By similarity). Localizes to the cell surface of ookinetes, especially
CC on the apical pellicle complex that is involved in invasion (By
CC similarity). When phosphorylated at Thr-339, localizes to the
CC cytoskeleton (By similarity). When phosphorylated at Ser-42, localizes
CC to the cytoplasm (By similarity). When ubiquitinated at Lys-138,
CC acetylated at Lys-133 and Lys-375 and phosphorylated at Tyr-139,
CC localizes to the food vacuole (By similarity). When triubiquitinated at
CC Lys-138, appears to colocalize with hemozoin in the food vacuole (By
CC similarity). {ECO:0000250|UniProtKB:Q7RA60,
CC ECO:0000250|UniProtKB:Q8IJN7, ECO:0000250|UniProtKB:W7JLR6}.
CC -!- DOMAIN: The pentapeptide insert motif is required for the stabilization
CC of the apo-enzyme in an active closed conformation, independently of
CC Mg(2+) binding. The motif is also required for homodimerization. This
CC motif is only present in Apicomplexa and plant enolases.
CC {ECO:0000250|UniProtKB:Q8IJN7}.
CC -!- DOMAIN: The DKSLVK motif binds to the lysine-binding Kringle domains of
CC plasminogen from various mammalian species. This motif is present only
CC in enolases of plant and several microbial pathogens including
CC Plasmodium species. {ECO:0000250|UniProtKB:W7JLR6}.
CC -!- SIMILARITY: Belongs to the enolase family. {ECO:0000305}.
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DR EMBL; AB026051; BAA76924.1; -; mRNA.
DR AlphaFoldDB; Q9UAL5; -.
DR SMR; Q9UAL5; -.
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 Acetylation; Cell membrane; Cytoplasm; Cytoskeleton; Glycolysis;
KW Isopeptide bond; Lyase; Magnesium; Membrane; Metal-binding; Nucleus;
KW Phosphoprotein; Ubl conjugation; Vacuole.
FT CHAIN 1..446
FT /note="Enolase"
FT /id="PRO_0000134091"
FT MOTIF 104..108
FT /note="Pentapeptide insert"
FT /evidence="ECO:0000250|UniProtKB:Q8IJN7"
FT MOTIF 277..282
FT /note="DKSLVK motif"
FT /evidence="ECO:0000250|UniProtKB:W7JLR6"
FT ACT_SITE 218
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT ACT_SITE 356
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT BINDING 42
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT BINDING 166
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT BINDING 175
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT BINDING 253
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT BINDING 304
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT BINDING 304
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT BINDING 331
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT BINDING 331
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT BINDING 383..386
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT BINDING 407
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IJN7"
FT MOD_RES 133
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q7RA60"
FT MOD_RES 139
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q7RA60"
FT MOD_RES 339
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q7RA60"
FT MOD_RES 375
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q7RA60"
FT CROSSLNK 138
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q7RA60"
SQ SEQUENCE 446 AA; 48662 MW; 85BCCBB006791073 CRC64;
MAHVITRINA REILDSRGNP TVEVDLETNL GIFRAAVPSG ASTGIYEALE LRDNDKSRYL
GKGVQKAIKN INEIIAPKLI GMNCTEQKKI DNLMVEELDG SKNEWGWSKS KLGANAILAI
SMAVCRAGAA ANKVSLYKYL AQLAGKKSDQ MVLPVPCLNV INGGSHAGNK LSFQEFMIVP
VGAPSFKEAL RYGAEVYHTL KSEIKKKYGI DATNVGDEGG FAPNILNANE ALDLLVTAIK
SAGYEGKVKI AMDVAASEFY NSENKTYDLD FKTPNNDKSL VKTGAQLVDL YIDLVKKYPI
VSIEDPFDQD DWENYAKLTA AIGKDVQIVG DDLLVTNPTR ITKALEKNAC NALPLKVNQI
GSITEAIEAC LLSQKNNWGV MVSHRSGETE DVFIADLVVA LRTGQIKTGA PCRSERNAKY
NQLLRIEESL GNNAVFAGEK FRLQLN
