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THIE_SYNPW
ID   THIE_SYNPW              Reviewed;         353 AA.
AC   A5GMH7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 74.
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};
GN   OrderedLocusNames=SynWH7803_1716;
OS   Synechococcus sp. (strain WH7803).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=32051;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WH7803;
RG   Genoscope;
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
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; CT971583; CAK24142.1; -; Genomic_DNA.
DR   RefSeq; WP_011933614.1; NC_009481.1.
DR   AlphaFoldDB; A5GMH7; -.
DR   SMR; A5GMH7; -.
DR   STRING; 32051.SynWH7803_1716; -.
DR   EnsemblBacteria; CAK24142; CAK24142; SynWH7803_1716.
DR   KEGG; syx:SynWH7803_1716; -.
DR   eggNOG; COG0352; Bacteria.
DR   HOGENOM; CLU_064900_0_0_3; -.
DR   OMA; EEWCRFG; -.
DR   OrthoDB; 461201at2; -.
DR   UniPathway; UPA00060; UER00141.
DR   Proteomes; UP000001566; 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..353
FT                   /note="Thiamine-phosphate synthase"
FT                   /id="PRO_1000052341"
FT   REGION          1..128
FT                   /note="Unknown"
FT   REGION          129..353
FT                   /note="Thiamine-phosphate synthase"
FT   BINDING         185..189
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         217
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         218
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01327"
FT   BINDING         237
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01327"
FT   BINDING         256
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         282..284
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         285
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         312
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         332..333
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   353 AA;  38820 MW;  0FB296A767D93919 CRC64;
     MESMPVAPST DPRVARLIDA NLDRAREGLR VIEDWCRFGL DRQDLVVPLK DWRQQLGQLH
     HDRYRQARST ATDSAAGLGH PAQDTRTDSV AIVKANASRV QEALRVIEEF ARNGDAVLAR
     TAAAVRYALY DHEVRILEAC GHSRRKQQLE DARLCLITDP GADDGCERLV QRVEAALQSG
     VSLVQYRRKH GSDGLRLQEA QQLAQLCHEH NALFIVNDRI DLALLVNADG VHLGQEDLPY
     REARRLLGSA KLIGRSTHKL AQLHEAQEQG ADYVGVGPVF ATATKADRHP AGLSWVKEAC
     EAARIPWFAI GGITATTLPR VREAGAQRVA VVSAIMASED PASASRQLLD LLT
 
 
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