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THIE_SYNSC
ID   THIE_SYNSC              Reviewed;         352 AA.
AC   Q3AL68;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=Syncc9605_0896;
OS   Synechococcus sp. (strain CC9605).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=110662;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC9605;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Schmutz J., Martinez M., Larimer F.,
RA   Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Synechococcus sp. CC9605.";
RL   Submitted (JUL-2005) 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; CP000110; ABB34664.1; -; Genomic_DNA.
DR   RefSeq; WP_011363888.1; NC_007516.1.
DR   AlphaFoldDB; Q3AL68; -.
DR   SMR; Q3AL68; -.
DR   STRING; 110662.Syncc9605_0896; -.
DR   EnsemblBacteria; ABB34664; ABB34664; Syncc9605_0896.
DR   KEGG; syd:Syncc9605_0896; -.
DR   eggNOG; COG0352; Bacteria.
DR   HOGENOM; CLU_064900_0_0_3; -.
DR   OMA; EEWCRFG; -.
DR   OrthoDB; 461201at2; -.
DR   UniPathway; UPA00060; UER00141.
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; Thiamine biosynthesis; Transferase.
FT   CHAIN           1..352
FT                   /note="Thiamine-phosphate synthase"
FT                   /id="PRO_1000052342"
FT   REGION          1..128
FT                   /note="Unknown"
FT   REGION          63..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          129..352
FT                   /note="Thiamine-phosphate synthase"
FT   BINDING         180..184
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         212
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         213
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01327"
FT   BINDING         232
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01327"
FT   BINDING         251
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         280
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         307
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   352 AA;  38642 MW;  0DAEE1F3C039B27C CRC64;
     MNPTPSETSL DPRVARLIDA NLDRAREGLR VVEDWCRFGL EQQDLVVRLK DWRQRLGRLH
     HDSYKQARST STDTGAGLKH PAQLDRHSPD RVVAANCARA QEALRVLEEY GRTIDPALAA
     EAAAIRYGLY DLEVTCLNAT LGARRRNKLK DACLCLITTP CDDLTDRVEA ALRNGVGMVQ
     YRCKAGNDRE RLQEAQQLRQ LCNKFGALLL INDRVDLALA VDADGVHLGQ EDMPSEVARD
     LLGVDRLLGR STHSIDQVHQ AQQEPIDYLG FGPIHSTAVK PERNPVGVEL LAKATAISQR
     PVFAIGGITP ANLPALLMAG GQRAAVIGAI MHSEDSGQAT RHLLQQLDQA TI
 
 
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