ID A0A0D9QLK9_PLAFR Unreviewed; 703 AA.
AC A0A0D9QLK9;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=pyruvate kinase {ECO:0000256|ARBA:ARBA00012142};
DE EC=2.7.1.40 {ECO:0000256|ARBA:ARBA00012142};
GN ORFNames=AK88_03787 {ECO:0000313|EMBL:KJP86591.1};
OS Plasmodium fragile.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX NCBI_TaxID=5857 {ECO:0000313|EMBL:KJP86591.1, ECO:0000313|Proteomes:UP000054561};
RN [1] {ECO:0000313|EMBL:KJP86591.1, ECO:0000313|Proteomes:UP000054561}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=nilgiri {ECO:0000313|Proteomes:UP000054561};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Neafsey D., Duraisingh M., Young S.K., Zeng Q., Gargeya S., Abouelleil A.,
RA Alvarado L., Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., Pearson M.,
RA Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Plasmodium fragile nilgiri.";
RL Submitted (MAR-2014) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KQ001690; KJP86591.1; -; Genomic_DNA.
DR RefSeq; XP_012336820.1; XM_012481397.1.
DR AlphaFoldDB; A0A0D9QLK9; -.
DR EnsemblProtists; KJP86591; KJP86591; AK88_03787.
DR GeneID; 24269101; -.
DR VEuPathDB; PlasmoDB:AK88_03787; -.
DR OMA; MIMPIEV; -.
DR OrthoDB; 1328317at2759; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000054561; 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, ECO:0000313|EMBL:KJP86591.1};
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, ECO:0000313|EMBL:KJP86591.1};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KJP86591.1}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..703
FT /note="pyruvate kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002344068"
FT DOMAIN 90..310
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 414..533
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 582..678
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
SQ SEQUENCE 703 AA; 80466 MW; BBA8AE8A35CC1A58 CRC64;
MKPKRFLLVA HLATLLVKGM VTYDGANTPF SKAHIQRCCS GGQLFLSNPH ITKQIRRKKS
IKVHTQTADL DIENKANTSR LSKKDKIAFT KTKQIATIGP ATEKFEELEK LYLSGIDVFR
LNFSHGLKSI KKYIINSLRI IEKKYDTSIG ILGDIQGPKI RIGEFEKSEK NAMEKNTFVE
LKEGDVFSFD LVDKPGNEKR VQLNYPELLK NIKCGQIILL DDGNLKMKVT EVQFDESSLQ
NSSLKVEVIT GGKLYSKKGF CVPNMIMPIE VLNEKDIKDI LFCINEGVDF LGYSFVQTKY
DLIFLKSIIK DYYDSDFFQN KVKKDRLIYD ENMLQMKEYD DPNDFYIKEV NDYYQHYYLK
NYQKYKQIYD VYKNQDLQVD NEKTENDLEN SGAGQNTAYD GDTQITHIKA ETDRSIPSDH
ANRIFIVSKI EKPSAVKNIE SIINLSDAIM IARGDLGIET NLSNLPILQK KLINLCRIKY
NKPVIVATQM MESMRFLPSP TRAEVADVAT ALYDGSDCVM LSAETATGQY PILTASTQNS
IIKDVENDYY YYDYTQRKNN NLVKCAHTMS PPPTNENSHF EKLIYSIRDI SNNINLKSII
LFSNEFHKIQ KLSNLRTKAP IIVITENVAL ARKLQLTWGV YPYITKLTDC HNQDLLTLIN
YGCKVSKEEG FVTQPEEYSL VTFTKNINNS SNLLYLCQPC LTT
//
