ID   A0A1H7J004_9BURK        Unreviewed;       612 AA.
AC   A0A1H7J004;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Thiamine-phosphate diphosphorylase {ECO:0000313|EMBL:SEK68059.1};
GN   ORFNames=SAMN05216359_102654 {ECO:0000313|EMBL:SEK68059.1};
OS   Roseateles sp. YR242.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sphaerotilaceae; Roseateles.
OX   NCBI_TaxID=1855305 {ECO:0000313|EMBL:SEK68059.1, ECO:0000313|Proteomes:UP000198631};
RN   [1] {ECO:0000313|EMBL:SEK68059.1, ECO:0000313|Proteomes:UP000198631}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YR242 {ECO:0000313|EMBL:SEK68059.1,
RC   ECO:0000313|Proteomes:UP000198631};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + ATP = 4-
CC         amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + ADP;
CC         Xref=Rhea:RHEA:19893, ChEBI:CHEBI:30616, ChEBI:CHEBI:57841,
CC         ChEBI:CHEBI:58354, ChEBI:CHEBI:456216; EC=2.7.4.7;
CC         Evidence={ECO:0000256|ARBA:ARBA00000565};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-amino-5-hydroxymethyl-2-methylpyrimidine + ATP = 4-amino-2-
CC         methyl-5-(phosphooxymethyl)pyrimidine + ADP + H(+);
CC         Xref=Rhea:RHEA:23096, ChEBI:CHEBI:15378, ChEBI:CHEBI:16892,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58354, ChEBI:CHEBI:456216;
CC         EC=2.7.1.49; Evidence={ECO:0000256|ARBA:ARBA00000151};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004948}.
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DR   EMBL; FOAV01000002; SEK68059.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H7J004; -.
DR   STRING; 1855305.SAMN05216359_102654; -.
DR   OrthoDB; 9810880at2; -.
DR   UniPathway; UPA00060; UER00138.
DR   Proteomes; UP000198631; Unassembled WGS sequence.
DR   GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro.
DR   GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd01169; HMPP_kinase; 1.
DR   CDD; cd00564; TMP_TenI; 1.
DR   Gene3D; 3.40.1190.20; -; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR004399; HMP/HMP-P_kinase_dom.
DR   InterPro; IPR013749; PM/HMP-P_kinase-1.
DR   InterPro; IPR029056; Ribokinase-like.
DR   InterPro; IPR036206; ThiamineP_synth_sf.
DR   InterPro; IPR022998; ThiamineP_synth_TenI.
DR   PANTHER; PTHR20858:SF17; HYDROXYMETHYLPYRIMIDINE_PHOSPHOMETHYLPYRIMIDINE KINASE THI20-RELATED; 1.
DR   PANTHER; PTHR20858; PHOSPHOMETHYLPYRIMIDINE KINASE; 1.
DR   Pfam; PF08543; Phos_pyr_kin; 1.
DR   Pfam; PF02581; TMP-TENI; 1.
DR   SUPFAM; SSF53613; Ribokinase-like; 1.
DR   SUPFAM; SSF51391; Thiamin phosphate synthase; 1.
PE   4: Predicted;
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977}.
FT   DOMAIN          65..313
FT                   /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT                   /evidence="ECO:0000259|Pfam:PF08543"
FT   DOMAIN          396..584
FT                   /note="Thiamine phosphate synthase/TenI"
FT                   /evidence="ECO:0000259|Pfam:PF02581"
FT   REGION          355..387
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        355..386
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   612 AA;  64394 MW;  2B9432A02E355B55 CRC64;
     MPMRRAVFDI NDMTARATPT DLPRLWPHPS LPSPWAGTVD PWQESLTPWA GAATPAVVWS
     VAGTDSGGGA GLAADTRAAS AMGVHLCTVV AAITAQNSMG VQAVHPVAAA ALRAQLQALR
     ADLPARVIKT GLLASAAAVD VLLAQREDAC LVVDPVLGAS AGGAAFCDDA LLAAYRHQLL
     PQAALVTPNR REAERLLGVA AGQCGVPELA RRLRQLGAQA VCITGGDDTS QGTALALDWL
     DSPMASGWIA LPRLTAEPGQ ALHHHGSGCT FATAAAAALA RGFPVPDAVI LAKMLAWTAL
     RDGHAAGAGA GPLRPSPAFI NDPAALPVMG QADEEVLSDL LMQRWTQALQ QRLEPAQHKP
     LQPSTQTQTP WHPPSQGPSI APSQRGSSAD FRPGLYAITD QSARIPALAA SGHFAHIQLR
     IKQAAKPAQG DSAPLPLRDS IRAALGAVEG LDTTLWINDH WRLALEEGAR ALHLGQEDWT
     TLTLPERHDL WTRCQAGMLK LGLSSHSLWE LCRARAVSPT YIACGPVWPT TTKDMPWLPQ
     GLAQLRWWAR MAGRPVVAIG GILAPSQVEA AQRAGASAVC LVRAAERWMA RPAATDPVAS
     PAGVPDPWPT YE
//