ID   TPK1_ORYSJ              Reviewed;         264 AA.
AC   Q5JK24; A0A0P0VCI1;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Thiamine pyrophosphokinase 1;
DE            Short=OsTPK1;
DE            EC=2.7.6.2;
DE   AltName: Full=Thiamine kinase 1;
GN   Name=TPK1; OrderedLocusNames=Os01g0931400, LOC_Os01g70580;
GN   ORFNames=OSJNBa0052O12.42-1, P0506E04.20-1;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12447438; DOI=10.1038/nature01184;
RA   Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y.,
RA   Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H.,
RA   Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M.,
RA   Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M.,
RA   Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T.,
RA   Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S.,
RA   Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H.,
RA   Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y.,
RA   Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S.,
RA   Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y.,
RA   Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S.,
RA   Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H.,
RA   Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
RT   "The genome sequence and structure of rice chromosome 1.";
RL   Nature 420:312-316(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
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 (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + thiamine = AMP + H(+) + thiamine diphosphate;
CC         Xref=Rhea:RHEA:11576, ChEBI:CHEBI:15378, ChEBI:CHEBI:18385,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58937, ChEBI:CHEBI:456215; EC=2.7.6.2;
CC   -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis;
CC       thiamine diphosphate from thiamine: step 1/1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the thiamine pyrophosphokinase family.
CC       {ECO:0000305}.
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DR   EMBL; AP003272; BAD87327.1; -; Genomic_DNA.
DR   EMBL; AP004330; BAD88183.1; -; Genomic_DNA.
DR   EMBL; AP008207; BAF07211.1; -; Genomic_DNA.
DR   EMBL; AP014957; BAS76043.1; -; Genomic_DNA.
DR   EMBL; AK105048; BAG97081.1; -; mRNA.
DR   RefSeq; XP_015621775.1; XM_015766289.1.
DR   AlphaFoldDB; Q5JK24; -.
DR   SMR; Q5JK24; -.
DR   STRING; 4530.OS01T0931400-02; -.
DR   PaxDb; Q5JK24; -.
DR   PRIDE; Q5JK24; -.
DR   EnsemblPlants; Os01t0931400-02; Os01t0931400-02; Os01g0931400.
DR   GeneID; 4326818; -.
DR   Gramene; Os01t0931400-02; Os01t0931400-02; Os01g0931400.
DR   KEGG; osa:4326818; -.
DR   eggNOG; KOG3153; Eukaryota.
DR   HOGENOM; CLU_044237_0_2_1; -.
DR   InParanoid; Q5JK24; -.
DR   OMA; HHLYMMT; -.
DR   OrthoDB; 1428589at2759; -.
DR   UniPathway; UPA00060; UER00597.
DR   Proteomes; UP000000763; Chromosome 1.
DR   Proteomes; UP000059680; Chromosome 1.
DR   ExpressionAtlas; Q5JK24; baseline and differential.
DR   Genevisible; Q5JK24; OS.
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; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006772; P:thiamine metabolic process; IEA:InterPro.
DR   CDD; cd07995; TPK; 1.
DR   Gene3D; 3.40.50.10240; -; 1.
DR   InterPro; IPR006282; Thi_PPkinase.
DR   InterPro; IPR016966; Thiamin_pyrophosphokinase_euk.
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   Pfam; PF04265; TPK_B1_binding; 1.
DR   Pfam; PF04263; TPK_catalytic; 1.
DR   PIRSF; PIRSF031057; Thiamin_pyrophosphokinase; 1.
DR   SMART; SM00983; TPK_B1_binding; 1.
DR   SUPFAM; SSF63862; SSF63862; 1.
DR   SUPFAM; SSF63999; SSF63999; 1.
DR   TIGRFAMs; TIGR01378; thi_PPkinase; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Reference proteome;
KW   Transferase.
FT   CHAIN           1..264
FT                   /note="Thiamine pyrophosphokinase 1"
FT                   /id="PRO_0000423968"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   264 AA;  29288 MW;  D5D19BD6102E2A07 CRC64;
     MPLPTMTHSS SFLRLPATSS PHPPPADDAS AAYAVVVLNQ RLPRFAPLLW DRARLRVCAD
     GGANRVFDGM PELLPAEDPD QVRMRYKPDV IKGDMDSIRP EVKEYYSNLG AEIVDESHDQ
     DTTDLHKCVS FITRNPPGSE ESNLYILVLG ALGGRFDHEM GNINVLYRFS NIRIVLLSDD
     CSIFLLPKTH SHEIHIERSI EGPHCGLIPM GSPSASTTTT GLRWNLDNTS MSYGGLISTS
     NIVEEETVRI TSDSDLIWTI SLRN