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ALF_PLAF7
ID   ALF_PLAF7               Reviewed;         369 AA.
AC   Q7KQL9; A0A144A3T1;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Fructose-bisphosphate aldolase {ECO:0000305};
DE            EC=4.1.2.13 {ECO:0000269|PubMed:26289816};
GN   Name=FBPA {ECO:0000305}; ORFNames=PF14_0425, PF3D7_1444800;
OS   Plasmodium falciparum (isolate 3D7).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX   NCBI_TaxID=36329;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3D7;
RX   PubMed=12368864; DOI=10.1038/nature01097;
RA   Gardner M.J., Hall N., Fung E., White O., Berriman M., Hyman R.W.,
RA   Carlton J.M., Pain A., Nelson K.E., Bowman S., Paulsen I.T., James K.D.,
RA   Eisen J.A., Rutherford K.M., Salzberg S.L., Craig A., Kyes S., Chan M.-S.,
RA   Nene V., Shallom S.J., Suh B., Peterson J., Angiuoli S., Pertea M.,
RA   Allen J., Selengut J., Haft D., Mather M.W., Vaidya A.B., Martin D.M.A.,
RA   Fairlamb A.H., Fraunholz M.J., Roos D.S., Ralph S.A., McFadden G.I.,
RA   Cummings L.M., Subramanian G.M., Mungall C., Venter J.C., Carucci D.J.,
RA   Hoffman S.L., Newbold C., Davis R.W., Fraser C.M., Barrell B.G.;
RT   "Genome sequence of the human malaria parasite Plasmodium falciparum.";
RL   Nature 419:498-511(2002).
RN   [2]
RP   FUNCTION, INTERACTION WITH TRAP AND MTRAP, AND DEVELOPMENTAL STAGE.
RX   PubMed=16321976; DOI=10.1074/jbc.m509807200;
RA   Baum J., Richard D., Healer J., Rug M., Krnajski Z., Gilberger T.W.,
RA   Green J.L., Holder A.A., Cowman A.F.;
RT   "A conserved molecular motor drives cell invasion and gliding motility
RT   across malaria life cycle stages and other apicomplexan parasites.";
RL   J. Biol. Chem. 281:5197-5208(2006).
RN   [3]
RP   FUNCTION, AND INTERACTION WITH TRAP; RH1; RH2B AND RH4.
RX   PubMed=22991428; DOI=10.1128/mbio.00292-12;
RA   Pal-Bhowmick I., Andersen J., Srinivasan P., Narum D.L., Bosch J.,
RA   Miller L.H.;
RT   "Binding of aldolase and glyceraldehyde-3-phosphate dehydrogenase to the
RT   cytoplasmic tails of Plasmodium falciparum merozoite duffy binding-like and
RT   reticulocyte homology ligands.";
RL   MBio 3:0-0(2012).
RN   [4]
RP   FUNCTION, AND INTERACTION WITH G ACTIN AND F ACTIN.
RX   PubMed=25261592; DOI=10.1016/j.molbiopara.2014.09.006;
RA   Diaz S.A., Martin S.R., Grainger M., Howell S.A., Green J.L., Holder A.A.;
RT   "Plasmodium falciparum aldolase and the C-terminal cytoplasmic domain of
RT   certain apical organellar proteins promote actin polymerization.";
RL   Mol. Biochem. Parasitol. 197:9-14(2014).
RN   [5]
RP   FUNCTION, AND INTERACTION WITH TRAP; MTRAP; RH1; RH2B; RH4; AMA1; EBA140;
RP   EBA175 AND EBA181.
RX   PubMed=27607074; DOI=10.1371/journal.pone.0161850;
RA   Diaz S.A., Martin S.R., Howell S.A., Grainger M., Moon R.W., Green J.L.,
RA   Holder A.A.;
RT   "The Binding of Plasmodium falciparum Adhesins and Erythrocyte Invasion
RT   Proteins to Aldolase Is Enhanced by Phosphorylation.";
RL   PLoS ONE 11:e0161850-e0161850(2016).
RN   [6] {ECO:0007744|PDB:4TR9}
RP   X-RAY CRYSTALLOGRAPHY (2.11 ANGSTROMS) IN COMPLEX WITH P.BERGHEI TRAP
RP   PEPTIDE (604-606) AND INHIBITOR, CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP   PATHWAY, AND SUBUNIT.
RX   PubMed=26289816; DOI=10.1186/s12936-015-0834-9;
RA   Nemetski S.M., Cardozo T.J., Bosch G., Weltzer R., O'Malley K., Ejigiri I.,
RA   Kumar K.A., Buscaglia C.A., Nussenzweig V., Sinnis P., Levitskaya J.,
RA   Bosch J.;
RT   "Inhibition by stabilization: targeting the Plasmodium falciparum aldolase-
RT   TRAP complex.";
RL   Malar. J. 14:324-324(2015).
CC   -!- FUNCTION: Plays a key role in glycolysis by catalyzing the cleavage of
CC       fructose 1,6-bisphosphate into dihydroxyacetone phosphate and
CC       glyceraldehyde 3-phosphate (PubMed:26289816). Independently of its
CC       catalytic activity, connects the actin filaments, and thus the
CC       actomyosin motor, to cell surface adhesins of the thrombospondin-
CC       related anonymous protein (TRAP), the erythrocyte binding ligand (EBL)
CC       and reticulocyte binding homolog (RH) protein families; this
CC       interaction is probably involved in transducing the motor force across
CC       the parasite surface required for sporozoite and ookinete gliding
CC       motility and merozoite invasion (PubMed:22991428, PubMed:25261592)
CC       (Probable). Stimulates actin polymerisation (PubMed:25261592).
CC       {ECO:0000269|PubMed:22991428, ECO:0000269|PubMed:25261592,
CC       ECO:0000269|PubMed:26289816, ECO:0000305|PubMed:16321976,
CC       ECO:0000305|PubMed:22991428, ECO:0000305|PubMed:27607074}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-
CC         phosphate + dihydroxyacetone phosphate; Xref=Rhea:RHEA:14729,
CC         ChEBI:CHEBI:32966, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=4.1.2.13;
CC         Evidence={ECO:0000269|PubMed:26289816};
CC   -!- ACTIVITY REGULATION: The cytoplasmic tail of TRAP and probably other
CC       adhesins acts as a competitive inhibitor as the binding sites of the
CC       glycolytic substrate fructose 1,6-bisphosphate and TRAP partially
CC       overlap. {ECO:0000269|PubMed:26289816}.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 4/4.
CC       {ECO:0000269|PubMed:26289816}.
CC   -!- SUBUNIT: Homotetramer (PubMed:26289816). Interacts with TRAP (via
CC       cytoplasmic domain); the interaction prevents substrate binding and
CC       thereby inhibits aldolase activity (PubMed:26289816, PubMed:16321976)
CC       (Probable). Interacts with MTRAP (via cytoplasmic domain); MTRAP
CC       phosphorylation may increase the binding to FBPA (PubMed:16321976).
CC       Interact with RH1 (via cytoplasmic domain) (PubMed:22991428,
CC       PubMed:27607074). Interacts with RH2b (via cytoplasmic domain)
CC       (PubMed:22991428, PubMed:27607074). Interacts with RH4 (via cytoplasmic
CC       domain) (PubMed:22991428, PubMed:27607074). Interacts with AMA1 (via
CC       cytoplasmic domain); the interaction is weak, however it may be
CC       increased upon AMA1 phosphorylation (PubMed:27607074). Interacts with
CC       EBA140 (via cytoplasmic domain); the interaction is weak
CC       (PubMed:27607074). Interacts with EBA175 (via cytoplasmic domain); the
CC       interaction is weak (PubMed:27607074). Interacts with EBA181 (via
CC       cytoplasmic domain); the interaction is weak (PubMed:27607074).
CC       Interacts with G-actin and F-actin (PubMed:25261592). May interact with
CC       ACT2/actin II; the interaction inhibits FBPA catalytic activity (By
CC       similarity). Interacts with human SLC4A1/band 3 (via N-terminus); the
CC       interaction inhibits FBPA catalytic activity (By similarity).
CC       {ECO:0000250|UniProtKB:Q27744, ECO:0000269|PubMed:16321976,
CC       ECO:0000269|PubMed:22991428, ECO:0000269|PubMed:25261592,
CC       ECO:0000269|PubMed:26289816, ECO:0000269|PubMed:27607074,
CC       ECO:0000305|PubMed:22991428}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P14223}.
CC       Membrane {ECO:0000250|UniProtKB:P14223}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P14223}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:P14223}. Host cell membrane
CC       {ECO:0000250|UniProtKB:Q27744}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P14223}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:P14223}.
CC   -!- DEVELOPMENTAL STAGE: Expressed during parasite asexual blood stages,
CC       including in schizonts (at protein level).
CC       {ECO:0000269|PubMed:16321976}.
CC   -!- SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase
CC       family. {ECO:0000305}.
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DR   EMBL; LN999946; CZU00144.1; -; Genomic_DNA.
DR   RefSeq; XP_001348599.1; XM_001348563.2.
DR   PDB; 4TR9; X-ray; 2.11 A; A/B/C/D=1-369, E=360-366, G=358-366.
DR   PDBsum; 4TR9; -.
DR   AlphaFoldDB; Q7KQL9; -.
DR   SMR; Q7KQL9; -.
DR   BioGRID; 1207364; 4.
DR   IntAct; Q7KQL9; 4.
DR   STRING; 5833.PF14_0425; -.
DR   SwissPalm; Q7KQL9; -.
DR   PRIDE; Q7KQL9; -.
DR   EnsemblProtists; CZU00144; CZU00144; PF3D7_1444800.
DR   GeneID; 812007; -.
DR   KEGG; pfa:PF3D7_1444800; -.
DR   VEuPathDB; PlasmoDB:PF3D7_1444800; -.
DR   HOGENOM; CLU_031243_0_0_1; -.
DR   InParanoid; Q7KQL9; -.
DR   OMA; DYREMLF; -.
DR   PhylomeDB; Q7KQL9; -.
DR   Reactome; R-PFA-114608; Platelet degranulation.
DR   Reactome; R-PFA-6798695; Neutrophil degranulation.
DR   Reactome; R-PFA-70171; Glycolysis.
DR   Reactome; R-PFA-70263; Gluconeogenesis.
DR   Reactome; R-PFA-70350; Fructose catabolism.
DR   UniPathway; UPA00109; UER00183.
DR   Proteomes; UP000001450; Chromosome 14.
DR   GO; GO:0005737; C:cytoplasm; IDA:GeneDB.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IDA:GeneDB.
DR   GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IDA:UniProtKB.
DR   GO; GO:0008154; P:actin polymerization or depolymerization; IDA:GeneDB.
DR   GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IBA:GO_Central.
DR   GO; GO:0006096; P:glycolytic process; IDA:UniProtKB.
DR   GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR029768; Aldolase_I_AS.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR000741; FBA_I.
DR   PANTHER; PTHR11627; PTHR11627; 1.
DR   Pfam; PF00274; Glycolytic; 1.
DR   PROSITE; PS00158; ALDOLASE_CLASS_I; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Actin-binding; Cytoplasm; Glycolysis; Host cell membrane;
KW   Host membrane; Lyase; Membrane; Reference proteome; Schiff base.
FT   CHAIN           1..369
FT                   /note="Fructose-bisphosphate aldolase"
FT                   /id="PRO_0000233386"
FT   ACT_SITE        195
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P00883"
FT   ACT_SITE        237
FT                   /note="Schiff-base intermediate with dihydroxyacetone-P"
FT                   /evidence="ECO:0000250|UniProtKB:P00883"
FT   BINDING         62
FT                   /ligand="beta-D-fructose 1,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:32966"
FT                   /evidence="ECO:0000250|UniProtKB:P00883"
FT   BINDING         152
FT                   /ligand="beta-D-fructose 1,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:32966"
FT                   /evidence="ECO:0000250|UniProtKB:P00883"
FT   SITE            369
FT                   /note="Necessary for preference for fructose 1,6-
FT                   bisphosphate over fructose 1-phosphate"
FT                   /evidence="ECO:0000250|UniProtKB:P00883"
FT   HELIX           16..29
FT                   /evidence="ECO:0007829|PDB:4TR9"
FT   STRAND          35..39
FT                   /evidence="ECO:0007829|PDB:4TR9"
FT   HELIX           43..52
FT                   /evidence="ECO:0007829|PDB:4TR9"
FT   HELIX           59..70
FT                   /evidence="ECO:0007829|PDB:4TR9"
FT   HELIX           75..77
FT                   /evidence="ECO:0007829|PDB:4TR9"
FT   STRAND          79..84
FT                   /evidence="ECO:0007829|PDB:4TR9"
FT   HELIX           86..89
FT                   /evidence="ECO:0007829|PDB:4TR9"
FT   STRAND          94..96
FT                   /evidence="ECO:0007829|PDB:4TR9"
FT   HELIX           99..105
FT                   /evidence="ECO:0007829|PDB:4TR9"
FT   STRAND          109..113
FT                   /evidence="ECO:0007829|PDB:4TR9"
FT   STRAND          118..120
FT                   /evidence="ECO:0007829|PDB:4TR9"
FT   STRAND          124..126
FT                   /evidence="ECO:0007829|PDB:4TR9"
FT   STRAND          128..130
FT                   /evidence="ECO:0007829|PDB:4TR9"
FT   HELIX           136..146
FT                   /evidence="ECO:0007829|PDB:4TR9"
FT   STRAND          150..157
FT                   /evidence="ECO:0007829|PDB:4TR9"
FT   HELIX           161..163
FT                   /evidence="ECO:0007829|PDB:4TR9"
FT   HELIX           168..187
FT                   /evidence="ECO:0007829|PDB:4TR9"
FT   STRAND          191..198
FT                   /evidence="ECO:0007829|PDB:4TR9"
FT   HELIX           206..226
FT                   /evidence="ECO:0007829|PDB:4TR9"
FT   HELIX           231..233
FT                   /evidence="ECO:0007829|PDB:4TR9"
FT   HELIX           253..267
FT                   /evidence="ECO:0007829|PDB:4TR9"
FT   STRAND          274..278
FT                   /evidence="ECO:0007829|PDB:4TR9"
FT   HELIX           284..295
FT                   /evidence="ECO:0007829|PDB:4TR9"
FT   STRAND          301..309
FT                   /evidence="ECO:0007829|PDB:4TR9"
FT   HELIX           310..320
FT                   /evidence="ECO:0007829|PDB:4TR9"
FT   HELIX           324..326
FT                   /evidence="ECO:0007829|PDB:4TR9"
FT   HELIX           327..346
FT                   /evidence="ECO:0007829|PDB:4TR9"
FT   HELIX           362..366
FT                   /evidence="ECO:0007829|PDB:4TR9"
SQ   SEQUENCE   369 AA;  40105 MW;  2AE9CDED4F5C96A4 CRC64;
     MAHCTEYMNA PKKLPADVAE ELATTAQKLV QAGKGILAAD ESTQTIKKRF DNIKLENTIE
     NRASYRDLLF GTKGLGKFIS GAILFEETLF QKNEAGVPMV NLLHNENIIP GIKVDKGLVN
     IPCTDEEKST QGLDGLAERC KEYYKAGARF AKWRTVLVID TAKGKPTDLS IHETAWGLAR
     YASICQQNRL VPIVEPEILA DGPHSIEVCA VVTQKVLSCV FKALQENGVL LEGALLKPNM
     VTAGYECTAK TTTQDVGFLT VRTLRRTVPP ALPGVVFLSG GQSEEEASVN LNSINALGPH
     PWALTFSYGR ALQASVLNTW QGKKENVAKA REVLLQRAEA NSLATYGKYK GGAGGENAGA
     SLYEKKYVY
 
 
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