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Database: UniProt
Entry: A0A059B9U1_EUCGR
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ID   A0A059B9U1_EUCGR        Unreviewed;       572 AA.
AC   A0A059B9U1;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=thiamine phosphate synthase {ECO:0000256|ARBA:ARBA00012830};
DE            EC=2.5.1.3 {ECO:0000256|ARBA:ARBA00012830};
GN   ORFNames=EUGRSUZ_G00559 {ECO:0000313|EMBL:KCW62962.1};
OS   Eucalyptus grandis (Flooded gum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX   NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW62962.1};
RN   [1] {ECO:0000313|EMBL:KCW62962.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW62962.1};
RA   Schmutz J., Hayes R., Myburg A., Tuskan G., Grattapaglia D., Rokhsar D.S.;
RT   "The genome of Eucalyptus grandis.";
RL   Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
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};
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};
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};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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}.
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DR   EMBL; KK198759; KCW62962.1; -; Genomic_DNA.
DR   RefSeq; XP_010065456.1; XM_010067154.2.
DR   AlphaFoldDB; A0A059B9U1; -.
DR   STRING; 71139.A0A059B9U1; -.
DR   EnsemblPlants; KCW62962; KCW62962; EUGRSUZ_G00559.
DR   GeneID; 104452688; -.
DR   Gramene; KCW62962; KCW62962; EUGRSUZ_G00559.
DR   KEGG; egr:104452688; -.
DR   eggNOG; KOG2598; Eukaryota.
DR   InParanoid; A0A059B9U1; -.
DR   OMA; GHIFPTN; -.
DR   OrthoDB; 5477821at2759; -.
DR   UniPathway; UPA00060; UER00141.
DR   GO; GO:0009507; C:chloroplast; IBA:GO_Central.
DR   GO; GO:0008902; F:hydroxymethylpyrimidine kinase activity; IBA:GO_Central.
DR   GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IBA:GO_Central.
DR   GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009228; P:thiamine biosynthetic process; IBA:GO_Central.
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   HAMAP; MF_00097; TMP_synthase; 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   InterPro; IPR034291; TMP_synthase.
DR   NCBIfam; TIGR00097; HMP-P_kinase; 1.
DR   NCBIfam; TIGR00693; thiE; 1.
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   3: Inferred from homology;
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          88..332
FT                   /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT                   /evidence="ECO:0000259|Pfam:PF08543"
FT   DOMAIN          362..547
FT                   /note="Thiamine phosphate synthase/TenI"
FT                   /evidence="ECO:0000259|Pfam:PF02581"
FT   REGION          17..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   572 AA;  60379 MW;  46EB389CE8B7F2B8 CRC64;
     MAFSATLSCT VFFNLHKNRS RSSPPPHPSP ISPEKLRRSR GGSASSRSRS GRIRSFGAME
     AAAEAPGACE SGGGMAKVPH VLTVAGSDSG AGAGIQADLK ACAARGVYCS TVITAVTAQN
     TVGVQGVDNV PEEFVAEQLE SVLSDMQVDV VKTGMLPSPG IVRILRKSLN KFPVKALVVD
     PVMVSTSGDV LAGPSVLAVF REELLPLADI VTPNLKEASA LLGGRQLETI ADMHSAVKLL
     HQMGPRHVLV KGGDLPGSCD AVDVFFDGER IHDLHAPRVK TRNTHGTGCT LASCIAAELA
     KGSSMLPAVQ VAKRFVENAL DYSKEISIGK GPQGPFDHFL MLNRKVHNFG KKMVLDPSDL
     FLYAVTDSGM NRKWGRSIED AVKAAIEGGA TIIQLREKDA ETRNFLEAAK SCMEVCHSRG
     VPLLINDRID IALACDADGV HVGQSDMPVR TARTLLGPEK IIGVSCKTPQ QAQQAYMDGA
     DYIGSGGIYP TNTKENNLTI GLEGLKAVCL SSKLPVVAIG GIGMSNAHAV MELGLPNLKG
     VAVVSALFDR ECISTEARKL YEVLSGAAPE VK
//
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