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THIE_VIBPA
ID   THIE_VIBPA              Reviewed;         204 AA.
AC   Q87JW8;
DT   23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-MAY-2003, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Thiamine-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00097};
DE            Short=TP synthase {ECO:0000255|HAMAP-Rule:MF_00097};
DE            Short=TPS {ECO:0000255|HAMAP-Rule:MF_00097};
DE            EC=2.5.1.3 {ECO:0000255|HAMAP-Rule:MF_00097};
DE   AltName: Full=Thiamine-phosphate pyrophosphorylase {ECO:0000255|HAMAP-Rule:MF_00097};
DE            Short=TMP pyrophosphorylase {ECO:0000255|HAMAP-Rule:MF_00097};
DE            Short=TMP-PPase {ECO:0000255|HAMAP-Rule:MF_00097};
GN   Name=thiE {ECO:0000255|HAMAP-Rule:MF_00097}; OrderedLocusNames=VPA0130;
OS   Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=223926;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIMD 2210633;
RX   PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA   Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA   Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA   Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT   "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT   distinct from that of V. cholerae.";
RL   Lancet 361:743-749(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_00097}.
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_00097};
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_00097};
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_00097};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00097};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00097};
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_00097}.
CC   -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00097}.
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DR   EMBL; BA000032; BAC61473.1; -; Genomic_DNA.
DR   RefSeq; NP_799640.1; NC_004605.1.
DR   RefSeq; WP_005482839.1; NC_004605.1.
DR   AlphaFoldDB; Q87JW8; -.
DR   SMR; Q87JW8; -.
DR   STRING; 223926.28808268; -.
DR   EnsemblBacteria; BAC61473; BAC61473; BAC61473.
DR   GeneID; 1190809; -.
DR   KEGG; vpa:VPA0130; -.
DR   PATRIC; fig|223926.6.peg.3090; -.
DR   eggNOG; COG0352; Bacteria.
DR   HOGENOM; CLU_018272_3_2_6; -.
DR   OMA; VSAICHA; -.
DR   UniPathway; UPA00060; UER00141.
DR   Proteomes; UP000002493; Chromosome 2.
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   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR036206; ThiamineP_synth_sf.
DR   InterPro; IPR022998; ThiamineP_synth_TenI.
DR   InterPro; IPR034291; TMP_synthase.
DR   Pfam; PF02581; TMP-TENI; 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..204
FT                   /note="Thiamine-phosphate synthase"
FT                   /id="PRO_0000157060"
FT   BINDING         35..39
FT                   /ligand="4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine"
FT                   /ligand_id="ChEBI:CHEBI:57841"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00097"
FT   BINDING         67
FT                   /ligand="4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine"
FT                   /ligand_id="ChEBI:CHEBI:57841"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00097"
FT   BINDING         68
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00097"
FT   BINDING         87
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00097"
FT   BINDING         106
FT                   /ligand="4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine"
FT                   /ligand_id="ChEBI:CHEBI:57841"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00097"
FT   BINDING         132..134
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_00097"
FT   BINDING         135
FT                   /ligand="4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine"
FT                   /ligand_id="ChEBI:CHEBI:57841"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00097"
FT   BINDING         163
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_00097"
FT   BINDING         183..184
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_00097"
SQ   SEQUENCE   204 AA;  21796 MW;  30ED16DCD5F62066 CRC64;
     MNAYRLYLVT DDQQDLPTLK HVVRKAVEGG VTMVQVREKH GDVREFIERA QAVKTILEGT
     GVPLIINDRV DVALAVDADG VHLGQSDMPA EIARQLIGPN KILGLSIETE DQLAEADSLP
     IDYIGLSAIF ATPTKTNTKK HWGIGGLKMA LNTTSLPIVA IGGINETNIP ALSATGVHGL
     ALVSAICHAE NPTKAAEYLL SLMD
 
 
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