TPK1_ARATH
ID TPK1_ARATH Reviewed; 267 AA.
AC B9DGU7; Q93Z45; Q9SRY1;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Thiamine pyrophosphokinase 1 {ECO:0000303|PubMed:17611796};
DE Short=AtTPK1 {ECO:0000303|PubMed:17611796};
DE EC=2.7.6.2 {ECO:0000269|PubMed:17611796};
DE AltName: Full=Thiamine kinase 1 {ECO:0000303|PubMed:17611796};
GN Name=TPK1 {ECO:0000303|PubMed:17611796};
GN OrderedLocusNames=At1g02880 {ECO:0000312|Araport:AT1G02880};
GN ORFNames=F22D16.12 {ECO:0000312|EMBL:AAF02878.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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 3).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
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=1.28 uM for thiamine {ECO:0000269|PubMed:17611796};
CC Vmax=9.6 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 37 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=3;
CC Name=1;
CC IsoId=B9DGU7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=B9DGU7-2; Sequence=VSP_053286;
CC Name=3;
CC IsoId=B9DGU7-3; Sequence=VSP_053285;
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves and 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; AC009525; AAF02878.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27488.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27489.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27490.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM59189.1; -; Genomic_DNA.
DR EMBL; AY058144; AAL25560.1; -; mRNA.
DR EMBL; AY101539; AAM26660.1; -; mRNA.
DR EMBL; AK317288; BAH19964.1; -; mRNA.
DR EMBL; AY085584; AAM62805.1; -; mRNA.
DR PIR; B86159; B86159.
DR RefSeq; NP_001321569.1; NM_001331362.1. [B9DGU7-3]
DR RefSeq; NP_563669.1; NM_100169.2. [B9DGU7-2]
DR RefSeq; NP_849579.1; NM_179248.1. [B9DGU7-3]
DR RefSeq; NP_849580.1; NM_179249.3. [B9DGU7-1]
DR AlphaFoldDB; B9DGU7; -.
DR SMR; B9DGU7; -.
DR STRING; 3702.AT1G02880.3; -.
DR iPTMnet; B9DGU7; -.
DR PaxDb; B9DGU7; -.
DR PRIDE; B9DGU7; -.
DR ProteomicsDB; 234459; -. [B9DGU7-1]
DR EnsemblPlants; AT1G02880.1; AT1G02880.1; AT1G02880. [B9DGU7-3]
DR EnsemblPlants; AT1G02880.2; AT1G02880.2; AT1G02880. [B9DGU7-2]
DR EnsemblPlants; AT1G02880.3; AT1G02880.3; AT1G02880. [B9DGU7-1]
DR EnsemblPlants; AT1G02880.5; AT1G02880.5; AT1G02880. [B9DGU7-3]
DR GeneID; 839303; -.
DR Gramene; AT1G02880.1; AT1G02880.1; AT1G02880. [B9DGU7-3]
DR Gramene; AT1G02880.2; AT1G02880.2; AT1G02880. [B9DGU7-2]
DR Gramene; AT1G02880.3; AT1G02880.3; AT1G02880. [B9DGU7-1]
DR Gramene; AT1G02880.5; AT1G02880.5; AT1G02880. [B9DGU7-3]
DR KEGG; ath:AT1G02880; -.
DR Araport; AT1G02880; -.
DR TAIR; locus:2024660; AT1G02880.
DR eggNOG; KOG3153; Eukaryota.
DR OMA; HHLYMMT; -.
DR PhylomeDB; B9DGU7; -.
DR BioCyc; MetaCyc:AT1G02880-MON; -.
DR UniPathway; UPA00060; UER00597.
DR PRO; PR:B9DGU7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; B9DGU7; baseline and differential.
DR Genevisible; B9DGU7; 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 1"
FT /id="PRO_0000423966"
FT VAR_SEQ 1..77
FT /note="MSAMDVMIHSSSFLLPCDETSTGTRYALVVLNQSLPRFTPLLWEHAKLRLCA
FT DGGANRIYDELPLFFPNEDALAIRN -> MKKNLYF (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_053285"
FT VAR_SEQ 1..3
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_053286"
SQ SEQUENCE 267 AA; 29879 MW; 9C1F54C74A7425EB CRC64;
MSAMDVMIHS SSFLLPCDET STGTRYALVV LNQSLPRFTP LLWEHAKLRL CADGGANRIY
DELPLFFPNE DALAIRNRYK PDVIKGDMDS IRRDVLDFYI NLGTKVIDES HDQDTTDLDK
CILYIRHSTL NQETSGLQIL ATGALGGRFD HEAGNLNVLY RYPDTRIVLL SDDCLIQLLP
KTHRHEIHIQ SSLEGPHCGL IPIGTPSAKT TTSGLQWDLS NTEMRFGGLI STSNLVKEEK
ITVESDSDLL WTISIKKTGL SIQDHTP
