THIE_PROMA
ID THIE_PROMA Reviewed; 346 AA.
AC Q7VAV5;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Thiamine-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_01327};
DE Short=TP synthase {ECO:0000255|HAMAP-Rule:MF_01327};
DE Short=TPS {ECO:0000255|HAMAP-Rule:MF_01327};
DE EC=2.5.1.3 {ECO:0000255|HAMAP-Rule:MF_01327};
DE AltName: Full=Thiamine-phosphate pyrophosphorylase {ECO:0000255|HAMAP-Rule:MF_01327};
DE Short=TMP pyrophosphorylase {ECO:0000255|HAMAP-Rule:MF_01327};
DE Short=TMP-PPase {ECO:0000255|HAMAP-Rule:MF_01327};
GN Name=thiE {ECO:0000255|HAMAP-Rule:MF_01327}; OrderedLocusNames=Pro_1348;
OS Prochlorococcus marinus (strain SARG / CCMP1375 / SS120).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=167539;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SARG / CCMP1375 / SS120;
RX PubMed=12917486; DOI=10.1073/pnas.1733211100;
RA Dufresne A., Salanoubat M., Partensky F., Artiguenave F., Axmann I.M.,
RA Barbe V., Duprat S., Galperin M.Y., Koonin E.V., Le Gall F., Makarova K.S.,
RA Ostrowski M., Oztas S., Robert C., Rogozin I.B., Scanlan D.J.,
RA Tandeau de Marsac N., Weissenbach J., Wincker P., Wolf Y.I., Hess W.R.;
RT "Genome sequence of the cyanobacterium Prochlorococcus marinus SS120, a
RT nearly minimal oxyphototrophic genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10020-10025(2003).
CC -!- FUNCTION: 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:0000255|HAMAP-Rule:MF_01327}.
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:0000255|HAMAP-Rule:MF_01327};
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:0000255|HAMAP-Rule:MF_01327};
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:0000255|HAMAP-
CC Rule:MF_01327};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01327};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01327};
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. {ECO:0000255|HAMAP-
CC Rule:MF_01327}.
CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family.
CC {ECO:0000255|HAMAP-Rule:MF_01327}.
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DR EMBL; AE017126; AAQ00392.1; -; Genomic_DNA.
DR RefSeq; NP_875739.1; NC_005042.1.
DR RefSeq; WP_011125499.1; NC_005042.1.
DR AlphaFoldDB; Q7VAV5; -.
DR SMR; Q7VAV5; -.
DR STRING; 167539.Pro_1348; -.
DR EnsemblBacteria; AAQ00392; AAQ00392; Pro_1348.
DR GeneID; 54200685; -.
DR KEGG; pma:Pro_1348; -.
DR PATRIC; fig|167539.5.peg.1414; -.
DR eggNOG; COG0352; Bacteria.
DR HOGENOM; CLU_064900_0_0_3; -.
DR OMA; EEWCRFG; -.
DR OrthoDB; 461201at2; -.
DR UniPathway; UPA00060; UER00141.
DR Proteomes; UP000001420; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00564; TMP_TenI; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_00097; TMP_synthase; 1.
DR HAMAP; MF_01327; TMP_synthase_cyanobact; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR036206; ThiamineP_synth_sf.
DR InterPro; IPR022998; ThiamineP_synth_TenI.
DR InterPro; IPR041397; ThiD2.
DR InterPro; IPR034291; TMP_synthase.
DR InterPro; IPR016229; TMP_synthase_cyanobac_bac.
DR Pfam; PF17792; ThiD2; 1.
DR Pfam; PF02581; TMP-TENI; 1.
DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1.
DR SUPFAM; SSF51391; SSF51391; 1.
DR TIGRFAMs; TIGR00693; thiE; 1.
PE 3: Inferred from homology;
KW Magnesium; Metal-binding; Reference proteome; Thiamine biosynthesis;
KW Transferase.
FT CHAIN 1..346
FT /note="Thiamine-phosphate synthase"
FT /id="PRO_0000157080"
FT REGION 1..125
FT /note="Unknown"
FT REGION 126..346
FT /note="Thiamine-phosphate synthase"
FT BINDING 177..181
FT /ligand="4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine"
FT /ligand_id="ChEBI:CHEBI:57841"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01327"
FT BINDING 209
FT /ligand="4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine"
FT /ligand_id="ChEBI:CHEBI:57841"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01327"
FT BINDING 210
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01327"
FT BINDING 229
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01327"
FT BINDING 248
FT /ligand="4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine"
FT /ligand_id="ChEBI:CHEBI:57841"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01327"
FT BINDING 274..276
FT /ligand="2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-
FT ylidene]ethyl phosphate"
FT /ligand_id="ChEBI:CHEBI:62899"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01327"
FT BINDING 277
FT /ligand="4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine"
FT /ligand_id="ChEBI:CHEBI:57841"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01327"
FT BINDING 304
FT /ligand="2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-
FT ylidene]ethyl phosphate"
FT /ligand_id="ChEBI:CHEBI:62899"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01327"
SQ SEQUENCE 346 AA; 38944 MW; 57B620FC6274564D CRC64;
MSVTPNPDQH VAQLIDANLD RAREGLRVIE DWCRFSLKNK DMVITLKNWR QQLGKEHYEI
YKNARSSSSD QSAGLSHPAQ KERILPQQIL SANFARIQEA LRVIEEFSRI SHPKLSKISA
QIRYEIYDLE VIILKISNLN MLDEKLKSCK LCLITRTHPE LIKTVLLALK AGVTMIQYRC
KETPDNQMIA EAKELASICK SYNSLFLIND RADIALAVDA DGVHLGQKDM PIQTARKIIG
HQKIIGLSTH SLEEIQNATS QGCNYIGIGP IFKTKSKQND LSLGIDFFSK INLKTNLPWF
AIGGINKDNI DKIKEVGIKR VAVINAIMGA EDPYLASKEL LGKLKK
