ENO_PLAYO
ID ENO_PLAYO Reviewed; 444 AA.
AC Q7RA60;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Enolase {ECO:0000303|PubMed:19642995};
DE Short=PfENO {ECO:0000303|PubMed:24009698};
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:0000303|PubMed:24009698}; ORFNames=PY06644;
OS Plasmodium yoelii yoelii.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Vinckeia).
OX NCBI_TaxID=73239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17XNL;
RX PubMed=12368865; DOI=10.1038/nature01099;
RA Carlton J.M., Angiuoli S.V., Suh B.B., Kooij T.W., Pertea M., Silva J.C.,
RA Ermolaeva M.D., Allen J.E., Selengut J.D., Koo H.L., Peterson J.D., Pop M.,
RA Kosack D.S., Shumway M.F., Bidwell S.L., Shallom S.J., van Aken S.E.,
RA Riedmuller S.B., Feldblyum T.V., Cho J.K., Quackenbush J., Sedegah M.,
RA Shoaibi A., Cummings L.M., Florens L., Yates J.R. III, Raine J.D.,
RA Sinden R.E., Harris M.A., Cunningham D.A., Preiser P.R., Bergman L.W.,
RA Vaidya A.B., van Lin L.H., Janse C.J., Waters A.P., Smith H.O., White O.R.,
RA Salzberg S.L., Venter J.C., Fraser C.M., Hoffman S.L., Gardner M.J.,
RA Carucci D.J.;
RT "Genome sequence and comparative analysis of the model rodent malaria
RT parasite Plasmodium yoelii yoelii.";
RL Nature 419:512-519(2002).
RN [2]
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=19642995; DOI=10.1186/1475-2875-8-179;
RA Bhowmick I.P., Kumar N., Sharma S., Coppens I., Jarori G.K.;
RT "Plasmodium falciparum enolase: stage-specific expression and sub-cellular
RT localization.";
RL Malar. J. 8:179-179(2009).
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=21600245; DOI=10.1016/j.molbiopara.2011.05.001;
RA Das S., Shevade S., LaCount D.J., Jarori G.K.;
RT "Plasmodium falciparum enolase complements yeast enolase functions and
RT associates with the parasite food vacuole.";
RL Mol. Biochem. Parasitol. 179:8-17(2011).
RN [4]
RP SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION
RP AT TYR-137 AND THR-337, ACETYLATION AT LYS-131 AND LYS-373, AND
RP UBIQUITINATION AT LYS-136.
RX PubMed=24009698; DOI=10.1371/journal.pone.0072687;
RA Shevade S., Jindal N., Dutta S., Jarori G.K.;
RT "Food vacuole associated enolase in plasmodium undergoes multiple post-
RT translational modifications: evidence for atypical ubiquitination.";
RL PLoS ONE 8:e72687-e72687(2013).
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:W7JLR6};
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:0000269|PubMed:24009698}. Cell surface
CC {ECO:0000250|UniProtKB:Q8IJN7}. Cell membrane
CC {ECO:0000269|PubMed:19642995}; Peripheral membrane protein
CC {ECO:0000305}; Cytoplasmic side {ECO:0000269|PubMed:19642995}. Vacuole
CC {ECO:0000269|PubMed:21600245, ECO:0000269|PubMed:24009698}.
CC Note=Partially localizes to the nucleus in rings and trophozoites.
CC Localization to the nucleus and food vacuole is higher in early and
CC mid-stage trophozoites compared to the late-stage trophozoites and
CC schizonts (By similarity). In the nucleus, localizes to heterochromatin
CC region (By similarity). In rings, nuclear localization is dependent on
CC the actin cytoskeleton (By similarity). In the trophozoite food
CC vacuole, colocalizes with hemozoin, a product of heme detoxification
CC (By similarity). Localizes to the cell surface of merozoites (By
CC similarity). In gametocytes, predominantly localizes to the actin
CC cytoskeleton (By similarity). In sporozoites, localizes to punctate
CC structures beneath the cell membrane (PubMed:19642995). Localizes to
CC the cell surface of ookinetes, especially on the apical pellicle
CC complex that is involved in invasion (By similarity). When
CC phosphorylated at Thr-337, localizes to the cytoskeleton
CC (PubMed:24009698). When phosphorylated at Ser-40, localizes to the
CC cytoplasm (By similarity). When ubiquitinated at Lys-136, acetylated at
CC Lys-131 and Lys-373 and phosphorylated at Tyr-137, localizes to the
CC food vacuole (PubMed:24009698). When triubiquitinated at Lys-136,
CC appears to colocalize with hemozoin in the food vacuole
CC (PubMed:24009698). {ECO:0000250|UniProtKB:Q8IJN7,
CC ECO:0000250|UniProtKB:W7JLR6, ECO:0000269|PubMed:19642995,
CC ECO:0000269|PubMed:24009698}.
CC -!- DEVELOPMENTAL STAGE: Expressed in sporozoites (mosquito salivary gland
CC stage) (at protein level). {ECO:0000269|PubMed:19642995}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAA18892.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AABL01002274; EAA18892.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q7RA60; -.
DR SMR; Q7RA60; -.
DR STRING; 73239.Q7RA60; -.
DR EnsemblProtists; EAA18892; EAA18892; EAA18892.
DR InParanoid; Q7RA60; -.
DR UniPathway; UPA00109; UER00187.
DR Proteomes; UP000008553; Unassembled WGS sequence.
DR GO; GO:0005856; C:cytoskeleton; IDA:UniProtKB.
DR GO; GO:0020020; C:food vacuole; IDA:UniProtKB.
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 Acetylation; Cell membrane; Cytoplasm; Cytoskeleton; Glycolysis;
KW Isopeptide bond; Lyase; Magnesium; Membrane; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Ubl conjugation; Vacuole.
FT CHAIN 1..444
FT /note="Enolase"
FT /id="PRO_0000134092"
FT MOTIF 102..106
FT /note="Pentapeptide insert"
FT /evidence="ECO:0000250|UniProtKB:Q8IJN7"
FT MOTIF 275..280
FT /note="DKSLVK motif"
FT /evidence="ECO:0000250|UniProtKB:W7JLR6"
FT ACT_SITE 216
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT ACT_SITE 354
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT BINDING 40
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT BINDING 164
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT BINDING 173
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT BINDING 251
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT BINDING 302
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT BINDING 302
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT BINDING 329
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT BINDING 329
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT BINDING 381..384
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT BINDING 405
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IJN7"
FT MOD_RES 131
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:24009698"
FT MOD_RES 137
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:24009698"
FT MOD_RES 337
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:24009698"
FT MOD_RES 373
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:24009698"
FT CROSSLNK 136
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:24009698"
SQ SEQUENCE 444 AA; 48916 MW; 5E9803FBAC6364AB CRC64;
MIINPKNYEH IFYSRGNPTV EVDLETTLGI FRAAVPSGAS TGIYEALELR DNDKSRYLGK
GVQQAIKNIN EIIAPKLIGL DCREQKKIDN MMVQELDGSK TEWGWSKSKL GANAILAISM
AICRAGAAAN KTSLYKYVAQ LAGKNTEKMI LPVPCLNVIN GGSHAGNKLS FQEFMIVPVG
APSFKEAMRY GAEVYHTLKS EIKKKYGIDA TNVGDEGGFA PNILNAHEAL DLLVASIKKA
GYENKVKIAM DVAASEFYNS ETKTYDLDFK TPNNDKSLVK TGQELVDLYI ELVKKYPIIS
IEDPFDQDDW ENYAKLTEAI GKDVQIVGDD LLVTNPTRIE KALEKKACNA LLLKVNQIGS
ITEAIEACLL SQKNNWGVMV SHRSGETEDV FIADLVVALR TGQIKTGAPC RSERNAKYNQ
LFRIEESLGA NGSFAGDKFR LQLN
