TPS1_BRANA
ID TPS1_BRANA Reviewed; 523 AA.
AC O48881;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Thiamine biosynthetic bifunctional enzyme BTH1, 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:9700068};
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=BTH1;
OS Brassica napus (Rape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=3708;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, AND INDUCTION.
RX PubMed=9700068; DOI=10.1023/a:1006030617502;
RA Kim Y.S., Nosaka K., Downs D.M., Kwak J.M., Park D., Chung I.K., Nam H.G.;
RT "A Brassica cDNA clone encoding a bifunctional hydroxymethylpyrimidine
RT kinase/thiamin-phosphate pyrophosphorylase involved in thiamin
RT biosynthesis.";
RL Plant Mol. Biol. 37:955-966(1998).
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:9700068}.
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:9700068};
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:9700068};
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; Evidence={ECO:0000269|PubMed:9700068};
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 -!- 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 {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves and stems.
CC {ECO:0000269|PubMed:9700068}.
CC -!- INDUCTION: Down-regulated by treatment with exogenous thiamine.
CC {ECO:0000269|PubMed:9700068}.
CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family.
CC {ECO:0000305}.
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DR EMBL; AF015310; AAC31298.1; -; mRNA.
DR PIR; T07834; T07834.
DR AlphaFoldDB; O48881; -.
DR SMR; O48881; -.
DR PRIDE; O48881; -.
DR BRENDA; 2.7.1.49; 944.
DR BRENDA; 2.7.4.7; 944.
DR UniPathway; UPA00060; UER00137.
DR UniPathway; UPA00060; UER00141.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008902; F:hydroxymethylpyrimidine kinase activity; IGI:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro.
DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IGI:UniProtKB.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009228; P:thiamine biosynthetic process; IGI:UniProtKB.
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; Thiamine biosynthesis;
KW Transferase; Transit peptide.
FT TRANSIT 1..38
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 39..523
FT /note="Thiamine biosynthetic bifunctional enzyme BTH1,
FT chloroplastic"
FT /id="PRO_0000420253"
FT BINDING 346..350
FT /ligand="4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine"
FT /ligand_id="ChEBI:CHEBI:57841"
FT /evidence="ECO:0000250"
FT BINDING 378
FT /ligand="4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine"
FT /ligand_id="ChEBI:CHEBI:57841"
FT /evidence="ECO:0000250"
FT BINDING 379
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 398
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 417
FT /ligand="4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine"
FT /ligand_id="ChEBI:CHEBI:57841"
FT /evidence="ECO:0000250"
FT BINDING 443..445
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 446
FT /ligand="4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine"
FT /ligand_id="ChEBI:CHEBI:57841"
FT /evidence="ECO:0000250"
FT BINDING 473
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 496..497
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"
SQ SEQUENCE 523 AA; 56045 MW; A9EFA395207EE4EB CRC64;
MQSLGGIRSW PATWRTTTAS MTTTTTESVR KVAQVLTVAG SDSGAGAGIQ ADIKVCAARG
VYCASVKTAV KAKNTRAVQS VHLLPPDSVS EQLKSVLSDF EVDVVKTGML PSPEIVEVLL
QNLSEYPVRA LVVDPVMVST SGHVLAGSSI LSIFRERLLP LADIITPNVK EASALLGGVR
IQTVAEMRSA AKSLHQMGPR FVLVKGGDLP DSSDSVDVYF DGNEFHELHS PRIATRNTHG
TGCTLASCIA AELAKGSNML SAVKVAKRFV DSALNYSKDI VIGSGMQGPF DHFLSLKDPQ
SYRQSTFKPD DLFLYAVTDS RMNKKWNRSI VDAVKAAIEG GATIIQLREK EAETREFLEE
AKSCVDICRS NGVCLLINDR FDIAIALDAD GVHVGQSDMP VDLVRSLLGP DKIIGVSCKT
QEQAHQAWKD GADYIGSGGV FPTNTKANNR TIGLDGLREV CKASKLPVVA IGGIGISNAE
SVMRIGEPNL KGVAVVSALF DQECVLTQAK KLHKTLTESK REH
