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Entry: A0A176J3T5_9BACI
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ID   A0A176J3T5_9BACI        Unreviewed;       215 AA.
AC   A0A176J3T5;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=Thiamine-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00097};
DE            Short=TP synthase {ECO:0000256|HAMAP-Rule:MF_00097};
DE            Short=TPS {ECO:0000256|HAMAP-Rule:MF_00097};
DE            EC=2.5.1.3 {ECO:0000256|HAMAP-Rule:MF_00097};
DE   AltName: Full=Thiamine-phosphate pyrophosphorylase {ECO:0000256|HAMAP-Rule:MF_00097};
DE            Short=TMP pyrophosphorylase {ECO:0000256|HAMAP-Rule:MF_00097};
DE            Short=TMP-PPase {ECO:0000256|HAMAP-Rule:MF_00097};
GN   Name=thiE {ECO:0000256|HAMAP-Rule:MF_00097,
GN   ECO:0000313|EMBL:KZZ83594.1};
GN   ORFNames=AS29_014885 {ECO:0000313|EMBL:KZZ83594.1};
OS   Bacillus sp. SJS.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1423321 {ECO:0000313|EMBL:KZZ83594.1, ECO:0000313|Proteomes:UP000028527};
RN   [1] {ECO:0000313|EMBL:KZZ83594.1, ECO:0000313|Proteomes:UP000028527}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SJS {ECO:0000313|EMBL:KZZ83594.1,
RC   ECO:0000313|Proteomes:UP000028527};
RA   Newman J.D., Stropko S.J., Pipes S.E.;
RT   "Bacillus sp. SJS genome.";
RL   Submitted (APR-2016) 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:0000256|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:0000256|ARBA:ARBA00000876, ECO:0000256|HAMAP-
CC         Rule:MF_00097, ECO:0000256|RuleBase:RU003826};
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, ECO:0000256|HAMAP-
CC         Rule:MF_00097, ECO:0000256|RuleBase:RU003826};
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, ECO:0000256|HAMAP-
CC         Rule:MF_00097, ECO:0000256|RuleBase:RU003826};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00097};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|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.
CC       {ECO:0000256|ARBA:ARBA00005165, ECO:0000256|HAMAP-Rule:MF_00097}.
CC   -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00097, ECO:0000256|RuleBase:RU003826}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KZZ83594.1}.
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DR   EMBL; JAQV02000024; KZZ83594.1; -; Genomic_DNA.
DR   RefSeq; WP_035409062.1; NZ_JAQV02000024.1.
DR   AlphaFoldDB; A0A176J3T5; -.
DR   STRING; 1423321.AS29_014885; -.
DR   eggNOG; COG0352; Bacteria.
DR   OrthoDB; 9812206at2; -.
DR   UniPathway; UPA00060; UER00141.
DR   Proteomes; UP000028527; Unassembled WGS sequence.
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; 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   NCBIfam; TIGR00693; thiE; 1.
DR   PANTHER; PTHR20857; THIAMINE-PHOSPHATE PYROPHOSPHORYLASE; 1.
DR   PANTHER; PTHR20857:SF15; THIAMINE-PHOSPHATE SYNTHASE; 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, ECO:0000256|HAMAP-Rule:MF_00097};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00097};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028527};
KW   Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977, ECO:0000256|HAMAP-
KW   Rule:MF_00097};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00097}.
FT   DOMAIN          12..196
FT                   /note="Thiamine phosphate synthase/TenI"
FT                   /evidence="ECO:0000259|Pfam:PF02581"
FT   BINDING         41..45
FT                   /ligand="4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine"
FT                   /ligand_id="ChEBI:CHEBI:57841"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00097"
FT   BINDING         77
FT                   /ligand="4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine"
FT                   /ligand_id="ChEBI:CHEBI:57841"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00097"
FT   BINDING         78
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00097"
FT   BINDING         97
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00097"
FT   BINDING         115
FT                   /ligand="4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine"
FT                   /ligand_id="ChEBI:CHEBI:57841"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00097"
FT   BINDING         141..143
FT                   /ligand="2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-
FT                   ylidene]ethyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:62899"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00097"
FT   BINDING         144
FT                   /ligand="4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine"
FT                   /ligand_id="ChEBI:CHEBI:57841"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00097"
FT   BINDING         173
FT                   /ligand="2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-
FT                   ylidene]ethyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:62899"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00097"
FT   BINDING         193..194
FT                   /ligand="2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-
FT                   ylidene]ethyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:62899"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00097"
SQ   SEQUENCE   215 AA;  22779 MW;  3CE3B2935C0018AD CRC64;
     MNRNRIKQHL ALYFIAGTQD CPNDIEEVVT GSIEGGITLF QFREKGKGSL HTADEIEQLA
     VRLMQICRNS NIPFIVNDDV ELALKIGADG IHVGQDDAKA SEIITRLNGM ILGVSVHSAE
     EAKRALADGA DYIGVGPVFP TSSKEDAKEA KGTAVIEEIK QAGIDIPMVG IGGITAENAK
     NVVMAGADGV SVISSISRSE NPAAAARALK KEITR
//
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