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
//