ID A0A0S3S0E4_PHAAN Unreviewed; 259 AA.
AC A0A0S3S0E4;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 08-OCT-2025, entry version 34.
DE RecName: Full=Thiamine pyrophosphokinase {ECO:0000256|PIRNR:PIRNR031057};
DE EC=2.7.6.2 {ECO:0000256|PIRNR:PIRNR031057};
GN Name=Vigan.04G395300 {ECO:0000313|EMBL:BAT86314.1};
GN ORFNames=VIGAN_04395300 {ECO:0000313|EMBL:BAT86314.1};
OS Vigna angularis var. angularis.
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=157739 {ECO:0000313|EMBL:BAT86314.1, ECO:0000313|Proteomes:UP000291084};
RN [1] {ECO:0000313|EMBL:BAT86314.1, ECO:0000313|Proteomes:UP000291084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Shumari {ECO:0000313|Proteomes:UP000291084};
RX PubMed=26616024; DOI=10.1038/srep16780;
RA Sakai H., Naito K., Ogiso-Tanaka E., Takahashi Y., Iseki K., Muto C.,
RA Satou K., Teruya K., Shiroma A., Shimoji M., Hirano T., Itoh T., Kaga A.,
RA Tomooka N.;
RT "The power of single molecule real-time sequencing technology in the de
RT novo assembly of a eukaryotic genome.";
RL Sci. Rep. 5:16780-16780(2015).
CC -!- FUNCTION: Catalyzes the phosphorylation of thiamine to thiamine
CC pyrophosphate (TPP). TPP is an active cofactor for enzymes involved in
CC glycolysis and energy production. Plant leaves require high levels of
CC TPP for photosynthesis and carbohydrate metabolism.
CC {ECO:0000256|ARBA:ARBA00025120}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=thiamine + ATP = thiamine diphosphate + AMP + H(+);
CC Xref=Rhea:RHEA:11576, ChEBI:CHEBI:15378, ChEBI:CHEBI:18385,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58937, ChEBI:CHEBI:456215; EC=2.7.6.2;
CC Evidence={ECO:0000256|ARBA:ARBA00052367};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11577;
CC Evidence={ECO:0000256|ARBA:ARBA00052367};
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis;
CC thiamine diphosphate from thiamine: step 1/1.
CC {ECO:0000256|ARBA:ARBA00005078, ECO:0000256|PIRNR:PIRNR031057}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000256|ARBA:ARBA00004514}.
CC -!- SIMILARITY: Belongs to the thiamine pyrophosphokinase family.
CC {ECO:0000256|ARBA:ARBA00006785, ECO:0000256|PIRNR:PIRNR031057}.
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DR EMBL; AP015037; BAT86314.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S3S0E4; -.
DR OrthoDB; 25149at2759; -.
DR UniPathway; UPA00060; UER00597.
DR Proteomes; UP000291084; Chromosome 4.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030975; F:thiamine binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004788; F:thiamine diphosphokinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006772; P:thiamine metabolic process; IEA:InterPro.
DR CDD; cd07995; TPK; 1.
DR FunFam; 2.60.120.320:FF:000001; Thiamine pyrophosphokinase; 1.
DR FunFam; 3.40.50.10240:FF:000001; Thiamine pyrophosphokinase; 1.
DR Gene3D; 3.40.50.10240; Thiamin pyrophosphokinase, catalytic domain; 1.
DR Gene3D; 2.60.120.320; Thiamin pyrophosphokinase, thiamin-binding domain; 1.
DR InterPro; IPR006282; Thi_PPkinase.
DR InterPro; IPR016966; Thiamin_pyrophosphokinase_euk.
DR InterPro; IPR007373; Thiamin_PyroPKinase_B1-bd.
DR InterPro; IPR036371; TPK_B1-bd_sf.
DR InterPro; IPR007371; TPK_catalytic.
DR InterPro; IPR036759; TPK_catalytic_sf.
DR NCBIfam; TIGR01378; thi_PPkinase; 1.
DR PANTHER; PTHR13622; THIAMIN PYROPHOSPHOKINASE; 1.
DR PANTHER; PTHR13622:SF8; THIAMIN PYROPHOSPHOKINASE 1; 1.
DR Pfam; PF04265; TPK_B1_binding; 1.
DR Pfam; PF04263; TPK_catalytic; 1.
DR PIRSF; PIRSF031057; Thiamin_pyrophosphokinase; 1.
DR SMART; SM00983; TPK_B1_binding; 1.
DR SUPFAM; SSF63999; Thiamin pyrophosphokinase, catalytic domain; 1.
DR SUPFAM; SSF63862; Thiamin pyrophosphokinase, substrate-binding domain; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR031057};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR031057};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR031057};
KW Reference proteome {ECO:0000313|Proteomes:UP000291084};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR031057}.
FT DOMAIN 186..250
FT /note="Thiamin pyrophosphokinase thiamin-binding"
FT /evidence="ECO:0000259|SMART:SM00983"
SQ SEQUENCE 259 AA; 28855 MW; E9B136EFC4E81D90 CRC64;
MDLMCHCSNF LLSPENPNAA CSLSLNYALV ILNQSLPRFA PLLWDHAHVR VCADGGANRV
YDEMPLFFPH QQPSHVRSRY KPDAIKGDMD SIRKEVLDFY AKLGTKIIDE SHDQDTTDLH
KCVIYIRDLS PKIDGSEQCI LVAGALGGRF DHEIGNINVL CRFPNTRIIL LSDDCLIHLL
PKNRYHKIFI QSSVEGPHCG LIPIGMPSGS STTTGLKWDL NETAMRFGGL ISTSNIVKGE
IVTVQSDSDL LWTISIKKP
//
