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ENO_PLAFA
ID   ENO_PLAFA               Reviewed;         446 AA.
AC   Q27727;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Enolase {ECO:0000303|PubMed:8125109};
DE            EC=4.2.1.11 {ECO:0000250|UniProtKB:W7JLR6};
DE   AltName: Full=2-phospho-D-glycerate hydro-lyase;
DE   AltName: Full=2-phosphoglycerate dehydratase;
GN   Name=ENO {ECO:0000303|PubMed:8125109};
OS   Plasmodium falciparum.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX   NCBI_TaxID=5833;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=8125109; DOI=10.1111/j.1432-1033.1994.tb18650.x;
RA   Read M., Hicks K.E., Sims P.F.G., Hyde J.E.;
RT   "Molecular characterisation of the enolase gene from the human malaria
RT   parasite Plasmodium falciparum. Evidence for ancestry within a
RT   photosynthetic lineage.";
RL   Eur. J. Biochem. 220:513-520(1994).
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; U00152; AAA18634.1; -; Unassigned_DNA.
DR   PIR; S42206; S42206.
DR   AlphaFoldDB; Q27727; -.
DR   SMR; Q27727; -.
DR   MoonProt; Q27727; -.
DR   VEuPathDB; PlasmoDB:PF3D7_1015900; -.
DR   VEuPathDB; PlasmoDB:Pf7G8-2_000301500; -.
DR   VEuPathDB; PlasmoDB:Pf7G8_100020300; -.
DR   VEuPathDB; PlasmoDB:PfCD01_100021100; -.
DR   VEuPathDB; PlasmoDB:PfDd2_100021300; -.
DR   VEuPathDB; PlasmoDB:PfGA01_100021200; -.
DR   VEuPathDB; PlasmoDB:PfGB4_100020900; -.
DR   VEuPathDB; PlasmoDB:PfGN01_100021500; -.
DR   VEuPathDB; PlasmoDB:PfHB3_100020300; -.
DR   VEuPathDB; PlasmoDB:PfIT_100019900; -.
DR   VEuPathDB; PlasmoDB:PfKE01_100021200; -.
DR   VEuPathDB; PlasmoDB:PfKH01_100020500; -.
DR   VEuPathDB; PlasmoDB:PfKH02_100021400; -.
DR   VEuPathDB; PlasmoDB:PfML01_100020200; -.
DR   VEuPathDB; PlasmoDB:PfNF135_100021300; -.
DR   VEuPathDB; PlasmoDB:PfNF166_100020800; -.
DR   VEuPathDB; PlasmoDB:PfNF54_100021100; -.
DR   VEuPathDB; PlasmoDB:PfSD01_100020600; -.
DR   VEuPathDB; PlasmoDB:PfSN01_100021300; -.
DR   VEuPathDB; PlasmoDB:PfTG01_100021100; -.
DR   BRENDA; 4.2.1.11; 4889.
DR   SABIO-RK; Q27727; -.
DR   UniPathway; UPA00109; UER00187.
DR   GO; GO:0005829; C:cytosol; IDA:CAFA.
DR   GO; GO:0020039; C:pellicle; IDA:CAFA.
DR   GO; GO:0000015; C:phosphopyruvate hydratase complex; IMP:CAFA.
DR   GO; GO:0000287; F:magnesium ion binding; IMP:CAFA.
DR   GO; GO:0004634; F:phosphopyruvate hydratase activity; IMP:CAFA.
DR   GO; GO:0042803; F:protein homodimerization activity; IMP:CAFA.
DR   GO; GO:0044403; P:biological process involved in symbiotic interaction; IDA:CAFA.
DR   GO; GO:0044409; P:entry into host; IDA:CAFA.
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   3: Inferred from homology;
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_0000134090"
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;  48704 MW;  C738905EAFB009A8 CRC64;
     MAHVITRINA REILDSRGNP TVEVDLETNL GIFRAAVPSG ASTGIYEALE LRDNDKSRYL
     GKGVQKAIKN INEIIAPKLI GMNCTEQKKI DNLMVEELDG SKNEWGWSKS KLGANAILAI
     SMAVCRAGAA PNKVSLYKYL AQLAGKKSDQ MVLPVPCLNV INGGSHAGNK LSFQEFMIVP
     VGAPSFKEAL RYGAEVYHTL KSEIKKKYGI DATNVGDEGG FAPNILNANE ALDLLVTAIK
     SAGYEGKVKI AMDVAASEFY NSENKTYDLD FKTPNNDKSL VKTGAQLVDL YIDLVKKYPI
     VSIEDPFDQD DWENYAKLTA AIGKDVQIVG DDLLVTNPTR ITKALEKNAC NALLLKVNQI
     GSITEAIEAC LLSQKNNWGV MVSHRSGETE DVFIADLVVA LRTGQIKTGA PCRSERNAKY
     NQLLRIEESL GNNAVFAGEK FRLQLN
 
 
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