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Entry: A0A1H7A907_9FIRM
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ID   A0A1H7A907_9FIRM        Unreviewed;       217 AA.
AC   A0A1H7A907;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
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   ORFNames=SAMN05660742_11214 {ECO:0000313|EMBL:SEJ62153.1};
OS   Propionispira arboris.
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC   Propionispira.
OX   NCBI_TaxID=84035 {ECO:0000313|EMBL:SEJ62153.1, ECO:0000313|Proteomes:UP000199662};
RN   [1] {ECO:0000313|EMBL:SEJ62153.1, ECO:0000313|Proteomes:UP000199662}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2179 {ECO:0000313|EMBL:SEJ62153.1,
RC   ECO:0000313|Proteomes:UP000199662};
RA   de Groot N.N.;
RL   Submitted (OCT-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}.
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DR   EMBL; FNZK01000012; SEJ62153.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H7A907; -.
DR   STRING; 84035.SAMN05660742_11214; -.
DR   UniPathway; UPA00060; UER00141.
DR   Proteomes; UP000199662; 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:SF23; THIAMINE BIOSYNTHETIC BIFUNCTIONAL ENZYME; 1.
DR   PANTHER; PTHR20857; THIAMINE-PHOSPHATE PYROPHOSPHORYLASE; 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:UP000199662};
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          14..196
FT                   /note="Thiamine phosphate synthase/TenI"
FT                   /evidence="ECO:0000259|Pfam:PF02581"
FT   BINDING         44..48
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         76
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="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00097"
FT   BINDING         96
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         142..144
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         145
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   217 AA;  23361 MW;  2310440710E4573D CRC64;
     MRSLGMENFK KTKIYALTDE ALSKGRSNLE VVDQLIQAGI TFLQYREKEK TAREMYEQCT
     AIRKMTRAAN VTFVIDDFVD LALAVDADGV HIGQDDLPVQ SVRKLIGPDK ILGLSTHCLA
     QLHLAEKSGF VDYIGVGPVF ATQTKKNVSA PVGLDFVKYA ATQGKLPFVA IGGIKEHNIA
     EVCGAGAQTM AVVSAIVGAE DIGAKVKSLQ SLMNISC
//
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