ID M3ZEF1_XIPMA Unreviewed; 260 AA.
AC M3ZEF1;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 28-JAN-2026, entry version 56.
DE RecName: Full=Thiamine pyrophosphokinase {ECO:0000256|PIRNR:PIRNR031057};
DE EC=2.7.6.2 {ECO:0000256|PIRNR:PIRNR031057};
OS Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Xiphophorus.
OX NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000000593.2, ECO:0000313|Proteomes:UP000002852};
RN [1] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA Walter R., Schartl M., Warren W.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX PubMed=23542700; DOI=10.1038/ng.2604;
RA Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA Postlethwait J.H., Warren W.C.;
RT "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT evolutionary adaptation and several complex traits.";
RL Nat. Genet. 45:567-572(2013).
RN [3] {ECO:0000313|Ensembl:ENSXMAP00000000593.2}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000000593.2};
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [4] {ECO:0000313|Ensembl:ENSXMAP00000000593.2}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000000593.2};
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- FUNCTION: Catalyzes the phosphorylation of thiamine to thiamine
CC pyrophosphate (TPP) utilizing UTP and therefore links the biosynthesis
CC of TPP to pyrimidines metabolism. By producing thiamine pyrophosphate,
CC a cofactor of the mitochondrial pyruvate dehydrogenase indirectly
CC regulates pyruvate oxidation and lipogenesis. Although it can also
CC catalyze thiamine phosphorylation using ATP and CTP in vitro, it does
CC so with significantly lower efficiency and without physiological
CC relevance evidence. {ECO:0000256|ARBA:ARBA00055888}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=thiamine + UTP = thiamine diphosphate + UMP + H(+);
CC Xref=Rhea:RHEA:79423, ChEBI:CHEBI:15378, ChEBI:CHEBI:18385,
CC ChEBI:CHEBI:46398, ChEBI:CHEBI:57865, ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00050898};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:79424;
CC Evidence={ECO:0000256|ARBA:ARBA00050898};
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 -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the thiamine pyrophosphokinase family.
CC {ECO:0000256|ARBA:ARBA00006785, ECO:0000256|PIRNR:PIRNR031057}.
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DR AlphaFoldDB; M3ZEF1; -.
DR FunCoup; M3ZEF1; 442.
DR STRING; 8083.ENSXMAP00000000593; -.
DR Ensembl; ENSXMAT00000000595.2; ENSXMAP00000000593.2; ENSXMAG00000000597.2.
DR eggNOG; KOG3153; Eukaryota.
DR GeneTree; ENSGT00390000016016; -.
DR HOGENOM; CLU_044237_0_1_1; -.
DR InParanoid; M3ZEF1; -.
DR OMA; HHLYMMT; -.
DR UniPathway; UPA00060; UER00597.
DR Proteomes; UP000002852; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-ARBA.
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:0141200; F:UTP thiamine diphosphokinase activity; IEA:RHEA.
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; 3.40.50.10240:FF:000006; Thiamin pyrophosphokinase 1; 1.
DR FunFam; 2.60.120.320:FF:000002; 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 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:UP000002852};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR031057}.
FT DOMAIN 177..249
FT /note="Thiamin pyrophosphokinase thiamin-binding"
FT /evidence="ECO:0000259|SMART:SM00983"
SQ SEQUENCE 260 AA; 28971 MW; 3933CD8657F4E952 CRC64;
KDYDHFTIIL CTSDYFRCFS VSGKQRICLI ILNQPIDKDH LHTLWGKALL RACADGGANQ
LYNITAGDRD NFLPDYISGD FDSITPEVKA FYADKGCKLI ETADQDLTDY TKCLVKMLEE
IQTRKLQVDT IVTLGGLAGR FDQTMASVET LFHAQSMTQL PVLIIQETSL ACLLRPGNHR
LGVNTSLEGE WCSLIPVGGP CQTVTTGLKW NLDKQVLQFG KLVSTSNTYE PTAPRSPRKP
VTVTTDQPLL WSMGIHINEK
//
