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Database: UniProt
Entry: W4J2P5_PLAFP
LinkDB: W4J2P5_PLAFP
Original site: W4J2P5_PLAFP 
ID   W4J2P5_PLAFP            Unreviewed;       744 AA.
AC   W4J2P5;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=pyruvate kinase {ECO:0000256|ARBA:ARBA00012142};
DE            EC=2.7.1.40 {ECO:0000256|ARBA:ARBA00012142};
GN   ORFNames=PFUGPA_01641 {ECO:0000313|EMBL:ETW56470.1};
OS   Plasmodium falciparum (isolate Palo Alto / Uganda).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX   NCBI_TaxID=57270 {ECO:0000313|EMBL:ETW56470.1, ECO:0000313|Proteomes:UP000019103};
RN   [1] {ECO:0000313|EMBL:ETW56470.1, ECO:0000313|Proteomes:UP000019103}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Palo Alto/Uganda {ECO:0000313|EMBL:ETW56470.1,
RC   ECO:0000313|Proteomes:UP000019103};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Neafsey D., Hoffman S., Volkman S., Rosenthal P., Walker B., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W.,
RA   Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J.,
RA   Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A.,
RA   Ireland A., Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W.,
RA   Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Annotation of Plasmodium falciparum Palo Alto/Uganda.";
RL   Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ETW56470.1, ECO:0000313|Proteomes:UP000019103}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Palo Alto/Uganda {ECO:0000313|EMBL:ETW56470.1,
RC   ECO:0000313|Proteomes:UP000019103};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Neafsey D., Cheeseman I., Volkman S., Adams J., Walker B., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA   Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Plasmodium falciparum Palo Alto/Uganda.";
RL   Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate;
CC         Xref=Rhea:RHEA:18157, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58702, ChEBI:CHEBI:456216;
CC         EC=2.7.1.40; Evidence={ECO:0000256|ARBA:ARBA00001174};
CC   -!- COFACTOR:
CC       Name=K(+); Xref=ChEBI:CHEBI:29103;
CC         Evidence={ECO:0000256|ARBA:ARBA00001958};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 5/5. {ECO:0000256|ARBA:ARBA00004997}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC   -!- SIMILARITY: Belongs to the pyruvate kinase family.
CC       {ECO:0000256|ARBA:ARBA00008663}.
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DR   EMBL; KI927304; ETW56470.1; -; Genomic_DNA.
DR   AlphaFoldDB; W4J2P5; -.
DR   EnsemblProtists; ETW56470; ETW56470; PFUGPA_01641.
DR   OMA; MIMPIEV; -.
DR   UniPathway; UPA00109; UER00188.
DR   Proteomes; UP000019103; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0030955; F:potassium ion binding; IEA:InterPro.
DR   GO; GO:0004743; F:pyruvate kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 2.
DR   Gene3D; 2.40.33.10; PK beta-barrel domain-like; 1.
DR   Gene3D; 3.40.1380.20; Pyruvate kinase, C-terminal domain; 1.
DR   InterPro; IPR001697; Pyr_Knase.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR   InterPro; IPR011037; Pyrv_Knase-like_insert_dom_sf.
DR   InterPro; IPR018209; Pyrv_Knase_AS.
DR   InterPro; IPR015793; Pyrv_Knase_brl.
DR   InterPro; IPR015795; Pyrv_Knase_C.
DR   InterPro; IPR036918; Pyrv_Knase_C_sf.
DR   InterPro; IPR015806; Pyrv_Knase_insert_dom_sf.
DR   PANTHER; PTHR11817:SF3; AT14039P-RELATED; 1.
DR   PANTHER; PTHR11817; PYRUVATE KINASE; 1.
DR   Pfam; PF00224; PK; 2.
DR   Pfam; PF02887; PK_C; 1.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   SUPFAM; SSF50800; PK beta-barrel domain-like; 1.
DR   SUPFAM; SSF52935; PK C-terminal domain-like; 1.
DR   PROSITE; PS00110; PYRUVATE_KINASE; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Pyruvate {ECO:0000256|ARBA:ARBA00023317};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019103};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..744
FT                   /note="pyruvate kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004844662"
FT   DOMAIN          98..318
FT                   /note="Pyruvate kinase barrel"
FT                   /evidence="ECO:0000259|Pfam:PF00224"
FT   DOMAIN          435..552
FT                   /note="Pyruvate kinase barrel"
FT                   /evidence="ECO:0000259|Pfam:PF00224"
FT   DOMAIN          626..720
FT                   /note="Pyruvate kinase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02887"
SQ   SEQUENCE   744 AA;  86571 MW;  9633003479CD244D CRC64;
     MNLIHICLFI IVIKCYVNCI KKNNKHIAYD KFYKQGSNTI VGSGNGSGDL LFLNNININK
     NVERKKNILA HSEIGTVRNI DDINLLNHNK KNEISFTKCK QIATIGPASE NFEQLEKLYL
     NGIDVFRLNF SHGLKSIKKY IINSIRILEK KYDTTIGILG DIQGPKIRIG EFEKNQINEN
     DNNTFVELKE GDLFSFDLMN SLGNQNRVQL NYPELIKNAK AGQIILLDDG NLKMKILENN
     YDTSNIQNSY IKVQVLTGGK LYSKKGFCIP NMIMPIDVLS EKDIKDILFC INEEVDFLGY
     SFVQTEYDLI FLRNIINDYY ESDFYNNIKR KDRINFDQNN LQMKTFDDEN DFYIKEVNDY
     YNNYYLKNVQ KYKQIYDVYK NQDLYINDNI QNHYNKNIVT NIGDDKNIID EQHIHNNNNN
     IDNIMKNYSN LYNINKDHNK IAIISKIEKP SAIKNIENII KLSDGIMIAR GDLGIETNLS
     NLPILQKKLI NLCRIKYNKP VIVATQMMES MRFLPSPTRA EVTDVATALY DGSDCVMLSA
     ETATGQYPIL TVSTQNKIIK DVENDYYYYE YTQRKNDKLK MLDHKNNCCH ENKDIQQINK
     YNHEYIQNNK YEQDIQNNIS YFDKLIFSIR DISNNINLKS IILFSNEFNK IQKLSNLRTK
     APIIVITENK YLARKLQLTW GIYPHLSKKQ NLFNHDLFSL INYGCDVSKK EGFVNSPDEY
     SLVTFSKNIN SANLLYLCQP CLTN
//
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