ENO_PLABA
ID ENO_PLABA Reviewed; 446 AA.
AC A0A509AQ68;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2019, sequence version 1.
DT 03-AUG-2022, entry version 16.
DE RecName: Full=Enolase {ECO:0000303|PubMed:21949403};
DE EC=4.2.1.11 {ECO:0000250|UniProtKB:Q8IJN7};
GN Name=ENO {ECO:0000250|UniProtKB:Q8IJN7};
GN ORFNames=PBANKA_1214300 {ECO:0000312|EMBL:VUC57042.1};
OS Plasmodium berghei (strain Anka).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Vinckeia).
OX NCBI_TaxID=5823 {ECO:0000312|Proteomes:UP000074855};
RN [1] {ECO:0000312|Proteomes:UP000074855}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANKA {ECO:0000312|Proteomes:UP000074855};
RX PubMed=25359557; DOI=10.1186/s12915-014-0086-0;
RA Otto T.D., Bohme U., Jackson A.P., Hunt M., Franke-Fayard B.,
RA Hoeijmakers W.A., Religa A.A., Robertson L., Sanders M., Ogun S.A.,
RA Cunningham D., Erhart A., Billker O., Khan S.M., Stunnenberg H.G.,
RA Langhorne J., Holder A.A., Waters A.P., Newbold C.I., Pain A., Berriman M.,
RA Janse C.J.;
RT "A comprehensive evaluation of rodent malaria parasite genomes and gene
RT expression.";
RL BMC Biol. 12:86-86(2014).
RN [2] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH HOST PLG, IDENTIFICATION
RP BY MASS SPECTROMETRY, DEVELOPMENTAL STAGE, AND BIOTECHNOLOGY.
RX PubMed=21949403; DOI=10.1073/pnas.1103657108;
RA Ghosh A.K., Coppens I., Gaardsvoll H., Ploug M., Jacobs-Lorena M.;
RT "Plasmodium ookinetes coopt mammalian plasminogen to invade the mosquito
RT midgut.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:17153-17158(2011).
RN [3] {ECO:0000305}
RP FUNCTION, INTERACTION WITH A.GAMBIAE EBP, SUBCELLULAR LOCATION,
RP DEVELOPMENTAL STAGE, AND BIOTECHNOLOGY.
RX PubMed=24474798; DOI=10.1073/pnas.1315517111;
RA Vega-Rodriguez J., Ghosh A.K., Kanzok S.M., Dinglasan R.R., Wang S.,
RA Bongio N.J., Kalume D.E., Miura K., Long C.A., Pandey A., Jacobs-Lorena M.;
RT "Multiple pathways for Plasmodium ookinete invasion of the mosquito
RT midgut.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:E492-E500(2014).
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 (PubMed:21949403, PubMed:24474798). Plays an essential
CC role during ookinete invasion of the mosquito vector midgut by
CC mediating the interaction of the ookinete with the midgut epithelium
CC and, further, by binding to mammalian host plasminogen in the blood
CC meal, whose conversion to active plasmin promotes the invasion process
CC (PubMed:21949403, PubMed:24474798). {ECO:0000250|UniProtKB:W7JLR6,
CC ECO:0000269|PubMed:21949403, ECO:0000269|PubMed:24474798}.
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 (PubMed:21949403). 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) (PubMed:24474798).
CC {ECO:0000250|UniProtKB:Q8IJN7, ECO:0000250|UniProtKB:W7JLR6,
CC ECO:0000269|PubMed:21949403, ECO:0000269|PubMed:24474798}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21949403}. Nucleus
CC {ECO:0000269|PubMed:21949403}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:W7JLR6}. Cell surface
CC {ECO:0000269|PubMed:21949403, ECO:0000269|PubMed:24474798}. Cell
CC membrane {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
CC (PubMed:21949403, PubMed:24474798). When phosphorylated at Thr-339,
CC localizes to the cytoskeleton (By similarity). When phosphorylated at
CC Ser-42, localizes to the cytoplasm (By similarity). When ubiquitinated
CC at Lys-138, acetylated at Lys-133 and Lys-375 and phosphorylated at
CC Tyr-139, localizes to the food vacuole (By similarity). When
CC triubiquitinated at Lys-138, appears to colocalize with hemozoin in the
CC food vacuole (By similarity). {ECO:0000250|UniProtKB:Q7RA60,
CC ECO:0000250|UniProtKB:Q8IJN7, ECO:0000250|UniProtKB:W7JLR6,
CC ECO:0000269|PubMed:21949403, ECO:0000269|PubMed:24474798}.
CC -!- DEVELOPMENTAL STAGE: Expressed in ookinetes (at protein level).
CC {ECO:0000269|PubMed:21949403, ECO:0000269|PubMed:24474798}.
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 -!- BIOTECHNOLOGY: The salivary gland and midgut peptide SM1 (PCQRAIFQSICK)
CC is a dodecapeptide that mimics enolase DKSLVK motif. By binding the EBP
CC receptor on the luminal surface of the female mosquito midgut
CC epithelium, SM1 inhibits ookinete invasion of P.berghei and thus, could
CC potentially be used to prevent parasite transmission by the mosquito
CC vector (PubMed:21949403, PubMed:24474798). Similarly, another peptide,
CC MP2 (ACYIKTLHPPCS), also inhibits ookinete invasion of P.berghei and
CC P.falciparum and could potentially be used to prevent parasite
CC transmission by the mosquito vector (PubMed:24474798).
CC {ECO:0000269|PubMed:21949403, ECO:0000269|PubMed:24474798}.
CC -!- SIMILARITY: Belongs to the enolase family. {ECO:0000305}.
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DR EMBL; LK023127; VUC57042.1; -; Genomic_DNA.
DR RefSeq; XP_676944.1; XM_671852.1.
DR SMR; A0A509AQ68; -.
DR STRING; 5823.A0A509AQ68; -.
DR VEuPathDB; PlasmoDB:PBANKA_1214300; -.
DR OMA; EFMIIPV; -.
DR UniPathway; UPA00109; UER00187.
DR Proteomes; UP000074855; Chromosome 12.
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..446
FT /note="Enolase"
FT /id="PRO_0000456087"
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:0000255|PIRSR:PIRSR001400-1"
FT ACT_SITE 356
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PIRSR:PIRSR001400-1"
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:0000255|PIRSR:PIRSR001400-2"
FT BINDING 175
FT /ligand="substrate"
FT /evidence="ECO:0000255|PIRSR:PIRSR001400-2"
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:0000255|PIRSR:PIRSR001400-2"
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:0000255|PIRSR:PIRSR001400-2"
FT BINDING 383..386
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT BINDING 407
FT /ligand="substrate"
FT /evidence="ECO:0000255|PIRSR:PIRSR001400-2"
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; 49026 MW; 19AD72381CC3ECC6 CRC64;
MAHVITRINA REILDSRGNP TVEVDLETTL GIFRAAVPSG ASTGIYEALE LRDNDKSRYL
GKGVQQAIKN INEIIAPKLI GLDCREQKKI DNMMVQELDG SKTEWGWSKS KLGANAILAI
SMAICRAGAA ANKTSLYKYL AQLAGKNTEK MILPVPCLNV INGGSHAGNK LSFQEFMIVP
VGAPSFKEAM RYGAEVYHTL KSEIKKKYGI DATNVGDEGG FAPNILNAHE ALDLLVASIK
KAGYENKVKI AMDVAASEFY NIETKTYDLD FKTPNNDKSL VKTGQELVDL YIELVKKYPI
ISIEDPFDQD DWENYAKLTE AIGKDVQIVG DDLLVTNPTR IEKALEKKAC NALLLKVNQI
GSITEAIEAC LLSQKNNWGV MVSHRSGETE DVFIADLVVA LRTGQIKTGA PCRSERNAKY
NQLFRIEESL GANGSFAGDK FRLQLN
