ID A0A3L6QXH3_PANMI Unreviewed; 322 AA.
AC A0A3L6QXH3;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 28-JAN-2026, entry version 19.
DE RecName: Full=thiamine diphosphokinase {ECO:0000256|ARBA:ARBA00013245};
DE EC=2.7.6.2 {ECO:0000256|ARBA:ARBA00013245};
GN ORFNames=C2845_PM08G12890 {ECO:0000313|EMBL:RLM91912.1};
OS Panicum miliaceum (Proso millet) (Broomcorn millet).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Panicodae; Paniceae; Panicinae; Panicum;
OC Panicum sect. Panicum.
OX NCBI_TaxID=4540 {ECO:0000313|EMBL:RLM91912.1, ECO:0000313|Proteomes:UP000275267};
RN [1] {ECO:0000313|Proteomes:UP000275267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30683860; DOI=10.1038/s41467-019-08409-5;
RA Zou C., Miki D., Li D., Tang Q., Xiao L., Rajput S., Deng P., Jia W.,
RA Huang R., Zhang M., Sun Y., Hu J., Fu X., Schnable P.S., Li F., Zhang H.,
RA Feng B., Zhu X., Liu R., Schnable J.C., Zhu J.-K., Zhang H.;
RT "The genome of broomcorn millet.";
RL Nat. Commun. 10:436-436(2019).
CC -!- FUNCTION: Catalyzes the phosphorylation of thiamine to thiamine
CC pyrophosphate (TPP). TPP is an active cofactor for enzymes involved in
CC glycolysis and energy production. Plant leaves require high levels of
CC TPP for photosynthesis and carbohydrate metabolism.
CC {ECO:0000256|ARBA:ARBA00025120}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000256|ARBA:ARBA00004514}.
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:RLM91912.1}.
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DR EMBL; PQIB02000010; RLM91912.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L6QXH3; -.
DR STRING; 4540.A0A3L6QXH3; -.
DR OrthoDB; 25149at2759; -.
DR Proteomes; UP000275267; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
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: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 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:SF6; THIAMINE PYROPHOSPHOKINASE 2; 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:UP000275267};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 183..254
FT /note="Thiamin pyrophosphokinase thiamin-binding"
FT /evidence="ECO:0000259|SMART:SM00983"
SQ SEQUENCE 322 AA; 36933 MW; CD392613118C6BAF CRC64;
MLWRTVRSMD VMMHSSSFLL PKLHRPANKS VKNYALVVLN QHLPRYMPRL WDHANLRICA
DGGANRIFYE MFQLTNDEDE KSTRNRYIPE IIEGDMDSIR PEGSKISDKS HNQETTDLHK
CISRIHHSTP EHEKHNLCVL VTGALGGRFD HEAANINVLY LFSDMRIVLL SDDCLIRLLP
KTHHHELYIE SSIEGPHCGL FPVGAPSTNT TTTGLKWNLS ESKMRFGSMI STSNIVQSEK
SLLKSIELDR DSQLSLLPTS RSKYIVSKNA CKKFANVIDN NGYLFSIWFP HDELPMEEFQ
IQTFMKKANV SLLPRLPCNR IL
//
