ID Q7RE71_PLAYO Unreviewed; 307 AA.
AC Q7RE71;
DT 15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2003, sequence version 1.
DT 08-NOV-2023, entry version 84.
DE RecName: Full=thiamine diphosphokinase {ECO:0000256|ARBA:ARBA00013245};
DE EC=2.7.6.2 {ECO:0000256|ARBA:ARBA00013245};
GN ORFNames=PY05196 {ECO:0000313|EMBL:EAA17193.1};
OS Plasmodium yoelii yoelii.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Vinckeia).
OX NCBI_TaxID=73239 {ECO:0000313|EMBL:EAA17193.1, ECO:0000313|Proteomes:UP000008553};
RN [1] {ECO:0000313|EMBL:EAA17193.1, ECO:0000313|Proteomes:UP000008553}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17XNL {ECO:0000313|EMBL:EAA17193.1,
RC ECO:0000313|Proteomes:UP000008553};
RX PubMed=12368865; DOI=10.1038/nature01099;
RA Carlton J.M., Angiuoli S.V., Suh B.B., Kooij T.W., Pertea M., Silva J.C.,
RA Ermolaeva M.D., Allen J.E., Selengut J.D., Koo H.L., Peterson J.D., Pop M.,
RA Kosack D.S., Shumway M.F., Bidwell S.L., Shallom S.J., van Aken S.E.,
RA Riedmuller S.B., Feldblyum T.V., Cho J.K., Quackenbush J., Sedegah M.,
RA Shoaibi A., Cummings L.M., Florens L., Yates J.R., Raine J.D., Sinden R.E.,
RA Harris M.A., Cunningham D.A., Preiser P.R., Bergman L.W., Vaidya A.B.,
RA van Lin L.H., Janse C.J., Waters A.P., Smith H.O., White O.R.,
RA Salzberg S.L., Venter J.C., Fraser C.M., Hoffman S.L., Gardner M.J.,
RA Carucci D.J.;
RT "Genome sequence and comparative analysis of the model rodent malaria
RT parasite Plasmodium yoelii yoelii.";
RL Nature 419:512-519(2002).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EAA17193.1}.
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DR EMBL; AABL01001638; EAA17193.1; -; Genomic_DNA.
DR AlphaFoldDB; Q7RE71; -.
DR STRING; 73239.Q7RE71; -.
DR PaxDb; 73239-Q7RE71; -.
DR EnsemblProtists; EAA17193; EAA17193; EAA17193.
DR InParanoid; Q7RE71; -.
DR OMA; NDECLSF; -.
DR Proteomes; UP000008553; 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:0030975; F:thiamine binding; IEA:InterPro.
DR GO; GO:0004788; F:thiamine diphosphokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:InterPro.
DR GO; GO:0006772; P:thiamine metabolic process; IEA:InterPro.
DR CDD; cd07995; TPK; 1.
DR Gene3D; 3.40.50.10240; Thiamin pyrophosphokinase, catalytic domain; 1.
DR Gene3D; 2.60.120.320; Thiamin pyrophosphokinase, thiamin-binding domain; 1.
DR InterPro; IPR006282; Thi_PPkinase.
DR InterPro; IPR007373; Thiamin_PyroPKinase_B1-bd.
DR InterPro; IPR036371; TPK_B1-bd_sf.
DR InterPro; IPR007371; TPK_catalytic.
DR InterPro; IPR036759; TPK_catalytic_sf.
DR NCBIfam; TIGR01378; thi_PPkinase; 1.
DR PANTHER; PTHR13622; THIAMIN PYROPHOSPHOKINASE; 1.
DR PANTHER; PTHR13622:SF8; THIAMIN PYROPHOSPHOKINASE 1; 1.
DR Pfam; PF04265; TPK_B1_binding; 1.
DR Pfam; PF04263; TPK_catalytic; 1.
DR SMART; SM00983; TPK_B1_binding; 1.
DR SUPFAM; SSF63999; Thiamin pyrophosphokinase, catalytic domain; 1.
DR SUPFAM; SSF63862; Thiamin pyrophosphokinase, substrate-binding domain; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000008553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 233..298
FT /note="Thiamin pyrophosphokinase thiamin-binding"
FT /evidence="ECO:0000259|SMART:SM00983"
SQ SEQUENCE 307 AA; 35737 MW; 6B8579C7BD201860 CRC64;
MEYFLSNYED QSSQIFKRKY ACSENTNDNG KFITIILNNV LCKNSSKILN KSDILICADG
GANRLYNLYK DIDKLENINN DKNEYLNCEN IKKNETETKL SNLFNKTIER DQEFENDVSQ
VGKKKKKFKH YPKILPDLIC GDFDSININV YNFYKKNNVL FEKCTDQNNT DLDKCIDKIK
HYVKKNDKIF ILGATGNRFD QTCANISSLY KKTLKNNIYL IGENNFLFLL KEGKHIININ
PNVFEKTCAL LPIGNKCKIK TEGLKYNLNY EYLSFDKLIS SSNEIIQTCI KISTDFPILY
NCYLKDL
//