ID   TPK2_ORYSJ              Reviewed;         267 AA.
AC   Q0JMW0; A0A0P0V2C5; Q5ZBJ5;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Thiamine pyrophosphokinase 2;
DE            Short=OsTPK2;
DE            EC=2.7.6.2;
DE   AltName: Full=Thiamine kinase 2;
GN   Name=TPK2; OrderedLocusNames=Os01g0356500, LOC_Os01g25440;
GN   ORFNames=B1157F09.24, P0025H06.10;
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD52763.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAD53067.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AP003207; BAD52763.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AP003312; BAD53067.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AP008207; BAF04918.1; -; Genomic_DNA.
DR   EMBL; AP014957; BAS72068.1; -; Genomic_DNA.
DR   EMBL; AK070843; BAG92167.1; -; mRNA.
DR   RefSeq; XP_015621862.1; XM_015766376.1.
DR   AlphaFoldDB; Q0JMW0; -.
DR   SMR; Q0JMW0; -.
DR   STRING; 4530.OS01T0356500-01; -.
DR   PaxDb; Q0JMW0; -.
DR   PRIDE; Q0JMW0; -.
DR   EnsemblPlants; Os01t0356500-01; Os01t0356500-01; Os01g0356500.
DR   GeneID; 4326288; -.
DR   Gramene; Os01t0356500-01; Os01t0356500-01; Os01g0356500.
DR   KEGG; osa:4326288; -.
DR   eggNOG; KOG3153; Eukaryota.
DR   HOGENOM; CLU_044237_0_2_1; -.
DR   InParanoid; Q0JMW0; -.
DR   OMA; ANLRICA; -.
DR   OrthoDB; 1428589at2759; -.
DR   UniPathway; UPA00060; UER00597.
DR   Proteomes; UP000000763; Chromosome 1.
DR   Proteomes; UP000059680; Chromosome 1.
DR   Genevisible; Q0JMW0; 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..267
FT                   /note="Thiamine pyrophosphokinase 2"
FT                   /id="PRO_0000423969"
SQ   SEQUENCE   267 AA;  30107 MW;  A21BDF30C4C59073 CRC64;
     MLGRAIRSME VMVHSSTFLL PKLHQPANSP AKKYALVVLN QNLPRFVPRL WTHAKLRICA
     DGGANRIFDE MFQMTNDPDY ESTRKRYIPE IIEGDMDSIR PEVKQFYSSQ GSKISDKSHN
     QETTDLHKCI SRIHRCTPDH EKTNLCVLVT GALGGRFDHE AANINILYLF SDMRIVLLSD
     DCLIRLLPKT HKHEIYIESS VEGPHCGLFP VGAPSGSTTT TGLKWNLSEA KMRFGSMIST
     SNIVHAEKVT VQSDADLLWT ISLRNLT