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Database: UniProt
Entry: A0A1S3VM52_VIGRR
LinkDB: A0A1S3VM52_VIGRR
Original site: A0A1S3VM52_VIGRR 
ID   A0A1S3VM52_VIGRR        Unreviewed;       564 AA.
AC   A0A1S3VM52;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=thiamine phosphate synthase {ECO:0000256|ARBA:ARBA00012830};
DE            EC=2.5.1.3 {ECO:0000256|ARBA:ARBA00012830};
GN   Name=LOC106776278 {ECO:0000313|RefSeq:XP_014519164.1};
OS   Vigna radiata var. radiata (Mung bean) (Phaseolus aureus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX   NCBI_TaxID=3916 {ECO:0000313|Proteomes:UP000087766, ECO:0000313|RefSeq:XP_014519164.1};
RN   [1] {ECO:0000313|RefSeq:XP_014519164.1}
RP   IDENTIFICATION.
RC   TISSUE=Leaf {ECO:0000313|RefSeq:XP_014519164.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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   RefSeq; XP_014519164.1; XM_014663678.2.
DR   AlphaFoldDB; A0A1S3VM52; -.
DR   STRING; 3916.A0A1S3VM52; -.
DR   GeneID; 106776278; -.
DR   KEGG; vra:106776278; -.
DR   OrthoDB; 5477821at2759; -.
DR   UniPathway; UPA00060; UER00141.
DR   Proteomes; UP000087766; Chromosome 10.
DR   GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro.
DR   GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC.
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   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   Reference proteome {ECO:0000313|Proteomes:UP000087766};
KW   Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          80..323
FT                   /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT                   /evidence="ECO:0000259|Pfam:PF08543"
FT   DOMAIN          354..538
FT                   /note="Thiamine phosphate synthase/TenI"
FT                   /evidence="ECO:0000259|Pfam:PF02581"
SQ   SEQUENCE   564 AA;  60582 MW;  3DF9C4A997545AAD CRC64;
     MASSESQLLR RHFDYGGAQV PPVLRRSSRF PFWKSVHANT DPNPKNHLSL RVKMQAQADT
     MMKPVSDNKI PHVLTVAGSD SGGGAGIQAD LKACAARRVY CSTVITAVTA QNTVGVQGVN
     IVPEDFVAEQ LQSVLSDMHV DVVKTGMLPS LNIVKVLCQT LRKFPVKALV VDPVMKSSSG
     DVLAGSSVLT GFLEELLPMT DIVTPNIKEA SVLLGDVPLK SVSDMRTAAK LIHDMGPRNV
     LVKGGDLPNS LDSVDVFFDG EEFYELCSPR INTRNSHGTG CTLASCIAAE LAKGSSMLSA
     VKTAKHFIDV ALDYSRDLAI GNGVQGPFDH FFELKNINHS SWRQNMFNPN DLLLYAVTDS
     GMNRKWGRSI AEAVKAAVEG GATIVQLREK DAETRDFLDA SKVCLEICRS YGVPLLINDR
     LDVALACDAD GVHVGQSDMP IRLARSLLGP EKIIGVSCKT PEQAHQAWID GADYIGCGGV
     YPTNTKANNR TIGLDGLKKV CEASKLPVVA IGGIGLSNAR AVMEIGEPNL KGVAVVSSLF
     DRECILTETR NLHALVSEPA LLIQ
//
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