TPK2_ARATH
ID TPK2_ARATH Reviewed; 267 AA.
AC F4IV16; O80514; Q94B25;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Thiamine pyrophosphokinase 2 {ECO:0000303|PubMed:17611796};
DE Short=AtTPK2 {ECO:0000303|PubMed:17611796};
DE EC=2.7.6.2 {ECO:0000269|PubMed:17611796};
DE AltName: Full=Thiamine kinase 2 {ECO:0000303|PubMed:17611796};
GN Name=TPK2 {ECO:0000303|PubMed:17611796};
GN OrderedLocusNames=At2g44750 {ECO:0000312|Araport:AT2G44750};
GN ORFNames=F16B22.24 {ECO:0000312|EMBL:AAC27477.2};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=17611796; DOI=10.1007/s11103-007-9205-4;
RA Ajjawi I., Rodriguez Milla M.A., Cushman J., Shintani D.K.;
RT "Thiamin pyrophosphokinase is required for thiamin cofactor activation in
RT Arabidopsis.";
RL Plant Mol. Biol. 65:151-162(2007).
CC -!- FUNCTION: Catalyzes the phosphorylation of thiamine to thiamine
CC pyrophosphate (TPP) (PubMed:17611796). TPP is an active cofactor for
CC enzymes involved in glycolysis and energy production (PubMed:17611796).
CC Plant leaves require high levels of TPP for photosynthesis and
CC carbohydrate metabolism (PubMed:17611796).
CC {ECO:0000269|PubMed:17611796}.
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 Evidence={ECO:0000269|PubMed:17611796};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11577;
CC Evidence={ECO:0000269|PubMed:17611796};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.96 uM for thiamine {ECO:0000269|PubMed:17611796};
CC Vmax=8.4 pmol/min/mg enzyme with thiamine as substrate
CC {ECO:0000269|PubMed:17611796};
CC pH dependence:
CC Optimum pH is 7. Active between pH 6 and pH 8.
CC {ECO:0000269|PubMed:17611796};
CC Temperature dependence:
CC Optimum temperature is 45 degrees Celsius.
CC {ECO:0000269|PubMed:17611796};
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis;
CC thiamine diphosphate from thiamine: step 1/1.
CC {ECO:0000269|PubMed:17611796}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:17611796}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=F4IV16-1; Sequence=Displayed;
CC Name=2;
CC IsoId=F4IV16-2; Sequence=VSP_053287;
CC -!- TISSUE SPECIFICITY: Expressed in leaves and at lower levels in flowers.
CC {ECO:0000269|PubMed:17611796}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions (PubMed:17611796). Tpk1 and tpk2 double mutants exhibit a
CC seedling lethal phenotype (PubMed:17611796).
CC {ECO:0000269|PubMed:17611796}.
CC -!- SIMILARITY: Belongs to the thiamine pyrophosphokinase family.
CC {ECO:0000305}.
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DR EMBL; AC003672; AAC27477.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC10463.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10464.1; -; Genomic_DNA.
DR EMBL; AY042898; AAK68838.1; -; mRNA.
DR EMBL; AY081493; AAM10055.1; -; mRNA.
DR PIR; T01602; T01602.
DR RefSeq; NP_566026.1; NM_130040.3. [F4IV16-2]
DR RefSeq; NP_850424.1; NM_180093.2. [F4IV16-1]
DR AlphaFoldDB; F4IV16; -.
DR SMR; F4IV16; -.
DR STRING; 3702.AT2G44750.2; -.
DR PaxDb; F4IV16; -.
DR PRIDE; F4IV16; -.
DR ProteomicsDB; 232405; -. [F4IV16-1]
DR EnsemblPlants; AT2G44750.1; AT2G44750.1; AT2G44750. [F4IV16-2]
DR EnsemblPlants; AT2G44750.2; AT2G44750.2; AT2G44750. [F4IV16-1]
DR GeneID; 819084; -.
DR Gramene; AT2G44750.1; AT2G44750.1; AT2G44750. [F4IV16-2]
DR Gramene; AT2G44750.2; AT2G44750.2; AT2G44750. [F4IV16-1]
DR KEGG; ath:AT2G44750; -.
DR Araport; AT2G44750; -.
DR TAIR; locus:2042436; AT2G44750.
DR eggNOG; KOG3153; Eukaryota.
DR OMA; ANLRICA; -.
DR OrthoDB; 1428589at2759; -.
DR PhylomeDB; F4IV16; -.
DR BioCyc; MetaCyc:AT2G44750-MON; -.
DR BRENDA; 2.7.6.2; 399.
DR UniPathway; UPA00060; UER00597.
DR PRO; PR:F4IV16; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; F4IV16; baseline and differential.
DR Genevisible; F4IV16; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
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; IDA:TAIR.
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; IGI:TAIR.
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 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cytoplasm; Kinase; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..267
FT /note="Thiamine pyrophosphokinase 2"
FT /id="PRO_0000423967"
FT VAR_SEQ 137..138
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_053287"
SQ SEQUENCE 267 AA; 30214 MW; 4EB8B19CE2F12699 CRC64;
MLSAMDVMIH SSSFLLPCDE TCGTRYALVV LNQNLPRFTP LLWEHAKLRL CADGGANRIY
DELPLFFPHE DPFVIRNRYK PDVIKGDMDS IRRDVLDFYV YWGTKVIDES HDQDTTDLDK
CISYIRHSTL NQESSRLQIL ATGALGGRFD HEAGNLNVLY RYPDTRIVLL SDDCLIQLLP
KTHRHEIHIH SSLQGPHCGL IPIGTPSANT TTSGLKWDLS NTEMRFGGLI STSNLVKEEI
ITVESDSDLL WTISIKKTGL PVQDHKP
