ID A0A1A8W1B2_9APIC Unreviewed; 547 AA.
AC A0A1A8W1B2;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=thiamine phosphate synthase {ECO:0000256|ARBA:ARBA00012830};
DE EC=2.5.1.3 {ECO:0000256|ARBA:ARBA00012830};
GN ORFNames=POVCU2_0031450 {ECO:0000313|EMBL:SBS85437.1};
OS Plasmodium ovale curtisi.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX NCBI_TaxID=864141 {ECO:0000313|EMBL:SBS85437.1, ECO:0000313|Proteomes:UP000078560};
RN [1] {ECO:0000313|Proteomes:UP000078560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Naeem Raeece;
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00000876};
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:0000256|ARBA:ARBA00001829};
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:0000256|ARBA:ARBA00001159};
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 {ECO:0000256|ARBA:ARBA00005165}.
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DR EMBL; FLQU01000421; SBS85437.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1A8W1B2; -.
DR UniPathway; UPA00060; UER00141.
DR Proteomes; UP000078560; Unassembled WGS sequence.
DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00564; TMP_TenI; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR HAMAP; MF_00097; TMP_synthase; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR036206; ThiamineP_synth_sf.
DR InterPro; IPR022998; ThiamineP_synth_TenI.
DR InterPro; IPR034291; TMP_synthase.
DR PANTHER; PTHR20857:SF15; THIAMINE BIOSYNTHETIC BIFUNCTIONAL ENZYME; 1.
DR PANTHER; PTHR20857; THIAMINE-PHOSPHATE PYROPHOSPHORYLASE; 1.
DR Pfam; PF02581; TMP-TENI; 1.
DR SUPFAM; SSF51391; Thiamin phosphate synthase; 1.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Reference proteome {ECO:0000313|Proteomes:UP000078560};
KW Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 27..237
FT /note="Thiamine phosphate synthase/TenI"
FT /evidence="ECO:0000259|Pfam:PF02581"
SQ SEQUENCE 547 AA; 62320 MW; 0FB994103A4F904D CRC64;
MAALPQGVMI KGRGLTTLSR KTVDYSLYLV TDDKFLKDKE NVCQTFMSKV REGILGGVKL
VQLRLKQADD LYFYNTAVQM KKELQRYNVP LIINNRLDIC LSVDADGVHV GKTDLPINIV
RKILGEKKMI GATINFSDEK DVEMAINNNV DYIAHEHTLY KSSTKETIAS YDQGIKKQIQ
ILRNKIKRLQ EKGKISKSLD ISLPPIILIG GINTRNIEET MATFYDSCAG VAVVSNIIGE
HYDSFLNALK LKFVVNKYKK NENMAFANLW ANYLRYFFYK TMENADREKN RTDFSVAEWS
NTDGVKTSNR EFVTTVPQGK LVTNVNFQKC VYNFVAKKIN FEAIPLGKTT QRYAEVGETI
FLFHSKCVNG GKGHYPRDSS GSNGKGNAYN DSVSEWVEKN KKEKMENNIF IFIGEELHEL
FKKKFSSTFF SLNYFFIITR RSQMHTGLFK QFDWDDMDTT SIEYSHNFIY IVLKNGYFND
DYKVTNLGVL LSYLLIAQGK TLPHFFSRIV GEGALARAGE KWLKFLGAVA TALEISVNEC
ARDEANA
//
