TPS1L_ARATH
ID TPS1L_ARATH Reviewed; 522 AA.
AC Q5M731; O23128; Q8L7M9;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Thiamine biosynthetic bifunctional enzyme TH1, chloroplastic;
DE Includes:
DE RecName: Full=Thiamine-phosphate synthase;
DE Short=TP synthase;
DE Short=TPS;
DE EC=2.5.1.3 {ECO:0000269|PubMed:16666289};
DE AltName: Full=Thiamine-phosphate pyrophosphorylase;
DE Short=TMP pyrophosphorylase;
DE Short=TMP-PPase;
DE Includes:
DE RecName: Full=Hydroxymethylpyrimidine kinase;
DE Short=HMP kinase;
DE EC=2.7.1.49 {ECO:0000250|UniProtKB:P30137};
DE Flags: Precursor;
GN Name=TH1; OrderedLocusNames=At1g22940; ORFNames=F19G10.10;
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].
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].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Cheuk R.F., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=cv. Columbia;
RX PubMed=16666289; DOI=10.1104/pp.88.2.248;
RA Komeda Y., Tanaka M., Nishimune T.;
RT "A th-1 mutant of Arabidopsis thaliana is defective for a thiamin-
RT phosphate-synthesizing enzyme: thiamin phosphate pyrophosphorylase.";
RL Plant Physiol. 88:248-250(1988).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP SER-63.
RX PubMed=17174261; DOI=10.1016/j.abb.2006.11.011;
RA Ajjawi I., Tsegaye Y., Shintani D.;
RT "Determination of the genetic, molecular, and biochemical basis of the
RT Arabidopsis thaliana thiamin auxotroph th1.";
RL Arch. Biochem. Biophys. 459:107-114(2007).
CC -!- FUNCTION: Essential for thiamine biosynthesis. Bifunctional enzyme that
CC catalyzes the phosphorylation of hydroxymethylpyrimidine phosphate
CC (HMP-P) to HMP-PP and condenses 4-methyl-5-(beta-hydroxyethyl)thiazole
CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine
CC pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
CC {ECO:0000269|PubMed:16666289, ECO:0000269|PubMed:17174261}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl
CC phosphate + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 2
CC H(+) = CO2 + diphosphate + thiamine phosphate; Xref=Rhea:RHEA:47844,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:37575, ChEBI:CHEBI:57841, ChEBI:CHEBI:62899; EC=2.5.1.3;
CC Evidence={ECO:0000269|PubMed:16666289};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate + 4-amino-2-
CC methyl-5-(diphosphooxymethyl)pyrimidine + 2 H(+) = CO2 + diphosphate
CC + thiamine phosphate; Xref=Rhea:RHEA:47848, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:33019, ChEBI:CHEBI:37575,
CC ChEBI:CHEBI:57841, ChEBI:CHEBI:62890; EC=2.5.1.3;
CC Evidence={ECO:0000269|PubMed:16666289};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 4-methyl-
CC 5-(2-phosphooxyethyl)-thiazole + H(+) = diphosphate + thiamine
CC phosphate; Xref=Rhea:RHEA:22328, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37575, ChEBI:CHEBI:57841,
CC ChEBI:CHEBI:58296; EC=2.5.1.3;
CC Evidence={ECO:0000269|PubMed:16666289};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-amino-5-hydroxymethyl-2-methylpyrimidine + ATP = 4-amino-2-
CC methyl-5-(phosphooxymethyl)pyrimidine + ADP + H(+);
CC Xref=Rhea:RHEA:23096, ChEBI:CHEBI:15378, ChEBI:CHEBI:16892,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58354, ChEBI:CHEBI:456216;
CC EC=2.7.1.49; Evidence={ECO:0000250|UniProtKB:P30137};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.8 uM for 2-methyl-4-amino-5-hydroxymethylpyrimidine diphosphate
CC {ECO:0000269|PubMed:16666289};
CC KM=2.7 uM for thiamine phosphate {ECO:0000269|PubMed:16666289};
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis;
CC thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine
CC and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1.
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; 4-
CC amino-2-methyl-5-diphosphomethylpyrimidine from 5-amino-1-(5-phospho-D-
CC ribosyl)imidazole: step 2/3.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:17174261}.
CC -!- DISRUPTION PHENOTYPE: Seedling lethality. Mutant plants can grow on
CC synthetic medium supplied with thiamine. {ECO:0000269|PubMed:17174261}.
CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB72162.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF000657; AAB72162.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE30313.1; -; Genomic_DNA.
DR EMBL; AY128364; AAM91567.1; -; mRNA.
DR EMBL; BT020417; AAV97808.1; -; mRNA.
DR PIR; E86363; E86363.
DR RefSeq; NP_173707.2; NM_102141.3.
DR AlphaFoldDB; Q5M731; -.
DR SMR; Q5M731; -.
DR STRING; 3702.AT1G22940.1; -.
DR PaxDb; Q5M731; -.
DR PRIDE; Q5M731; -.
DR ProteomicsDB; 228330; -.
DR EnsemblPlants; AT1G22940.1; AT1G22940.1; AT1G22940.
DR GeneID; 838901; -.
DR Gramene; AT1G22940.1; AT1G22940.1; AT1G22940.
DR KEGG; ath:AT1G22940; -.
DR Araport; AT1G22940; -.
DR TAIR; locus:2017734; AT1G22940.
DR eggNOG; KOG2598; Eukaryota.
DR HOGENOM; CLU_018272_7_0_1; -.
DR InParanoid; Q5M731; -.
DR OMA; GHIFPTN; -.
DR OrthoDB; 1245353at2759; -.
DR PhylomeDB; Q5M731; -.
DR BioCyc; ARA:AT1G22940-MON; -.
DR BioCyc; MetaCyc:AT1G22940-MON; -.
DR SABIO-RK; Q5M731; -.
DR UniPathway; UPA00060; UER00137.
DR UniPathway; UPA00060; UER00141.
DR PRO; PR:Q5M731; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q5M731; baseline and differential.
DR Genevisible; Q5M731; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008902; F:hydroxymethylpyrimidine kinase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IBA:GO_Central.
DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IDA:TAIR.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009228; P:thiamine biosynthetic process; IMP:TAIR.
DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd01169; HMPP_kinase; 1.
DR CDD; cd00564; TMP_TenI; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR Gene3D; 3.40.1190.20; -; 1.
DR HAMAP; MF_00097; TMP_synthase; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR045029; HMP/HMP-P_kinase.
DR InterPro; IPR004399; HMP/HMP-P_kinase_dom.
DR InterPro; IPR013749; PM/HMP-P_kinase-1.
DR InterPro; IPR029056; Ribokinase-like.
DR InterPro; IPR036206; ThiamineP_synth_sf.
DR InterPro; IPR022998; ThiamineP_synth_TenI.
DR InterPro; IPR034291; TMP_synthase.
DR PANTHER; PTHR20858; PTHR20858; 1.
DR Pfam; PF08543; Phos_pyr_kin; 1.
DR Pfam; PF02581; TMP-TENI; 1.
DR SUPFAM; SSF51391; SSF51391; 1.
DR SUPFAM; SSF53613; SSF53613; 1.
DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1.
DR TIGRFAMs; TIGR00693; thiE; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chloroplast; Kinase; Magnesium; Metal-binding;
KW Multifunctional enzyme; Nucleotide-binding; Plastid; Reference proteome;
KW Thiamine biosynthesis; Transferase; Transit peptide.
FT TRANSIT 1..36
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 37..522
FT /note="Thiamine biosynthetic bifunctional enzyme TH1,
FT chloroplastic"
FT /id="PRO_0000420252"
FT BINDING 345..349
FT /ligand="4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine"
FT /ligand_id="ChEBI:CHEBI:57841"
FT /evidence="ECO:0000250"
FT BINDING 377
FT /ligand="4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine"
FT /ligand_id="ChEBI:CHEBI:57841"
FT /evidence="ECO:0000250"
FT BINDING 378
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 397
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 416
FT /ligand="4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine"
FT /ligand_id="ChEBI:CHEBI:57841"
FT /evidence="ECO:0000250"
FT BINDING 442..444
FT /ligand="2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-
FT ylidene]ethyl phosphate"
FT /ligand_id="ChEBI:CHEBI:62899"
FT /evidence="ECO:0000250"
FT BINDING 445
FT /ligand="4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine"
FT /ligand_id="ChEBI:CHEBI:57841"
FT /evidence="ECO:0000250"
FT BINDING 472
FT /ligand="2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-
FT ylidene]ethyl phosphate"
FT /ligand_id="ChEBI:CHEBI:62899"
FT /evidence="ECO:0000250"
FT BINDING 495..496
FT /ligand="2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-
FT ylidene]ethyl phosphate"
FT /ligand_id="ChEBI:CHEBI:62899"
FT /evidence="ECO:0000250"
FT MUTAGEN 63
FT /note="S->F: In th1-201; loss of activity and seedling
FT lethality."
FT /evidence="ECO:0000269|PubMed:17174261"
FT CONFLICT 301
FT /note="S -> P (in Ref. 3; AAM91567)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 522 AA; 55813 MW; D10B8D6C34641B4A CRC64;
MNSLGGIRSW PANWRSTTAS MTTTESVRKV PQVLTVAGSD SGAGAGIQAD LKVCAARGVY
CASVITAVTA QNTRGVQSVH LLPPEFISEQ LKSVLSDFEF DVVKTGMLPS TEIVEVLLQN
LSDFPVRALV VDPVMVSTSG HVLAGSSILS IFRERLLPIA DIITPNVKEA SALLDGFRIE
TVAEMRSAAK SLHEMGPRFV LVKGGDLPDS SDSVDVYFDG KEFHELRSPR IATRNTHGTG
CTLASCIAAE LAKGSSMLSA VKVAKRFVDN ALDYSKDIVI GSGMQGPFDH FFGLKKDPQS
SRCSIFNPDD LFLYAVTDSR MNKKWNRSIV DALKAAIEGG ATIIQLREKE AETREFLEEA
KACIDICRSH GVSLLINDRI DIALACDADG VHVGQSDMPV DLVRSLLGPD KIIGVSCKTP
EQAHQAWKDG ADYIGSGGVF PTNTKANNRT IGLDGLKEVC EASKLPVVAI GGIGISNAGS
VMQIDAPNLK GVAVVSALFD QDCVLTQAKK LHKTLKESKR GI
