ID I3N387_ICTTR Unreviewed; 243 AA.
AC I3N387;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Thiamine pyrophosphokinase {ECO:0000256|PIRNR:PIRNR031057};
DE EC=2.7.6.2 {ECO:0000256|PIRNR:PIRNR031057};
GN Name=TPK1 {ECO:0000313|Ensembl:ENSSTOP00000018833.1};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000018833.1, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000018833.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + thiamine = AMP + H(+) + thiamine diphosphate;
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|PIRNR:PIRNR031057};
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 -!- SIMILARITY: Belongs to the thiamine pyrophosphokinase family.
CC {ECO:0000256|ARBA:ARBA00006785, ECO:0000256|PIRNR:PIRNR031057}.
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DR EMBL; AGTP01044987; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01044988; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01044989; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01044990; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01044991; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01044992; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01044993; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01044994; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01044995; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01044996; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_005326683.2; XM_005326626.2.
DR AlphaFoldDB; I3N387; -.
DR STRING; 43179.ENSSTOP00000018833; -.
DR Ensembl; ENSSTOT00000023272.2; ENSSTOP00000018833.1; ENSSTOG00000021109.2.
DR GeneID; 101967955; -.
DR CTD; 27010; -.
DR eggNOG; KOG3153; Eukaryota.
DR GeneTree; ENSGT00390000016016; -.
DR HOGENOM; CLU_044237_0_1_1; -.
DR InParanoid; I3N387; -.
DR OMA; TDMCKAL; -.
DR OrthoDB; 102116at2759; -.
DR TreeFam; TF313224; -.
DR UniPathway; UPA00060; UER00597.
DR Proteomes; UP000005215; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006772; P:thiamine metabolic process; IEA:Ensembl.
DR CDD; cd07995; TPK; 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:UP000005215};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR031057}.
FT DOMAIN 168..235
FT /note="Thiamin pyrophosphokinase thiamin-binding"
FT /evidence="ECO:0000259|SMART:SM00983"
SQ SEQUENCE 243 AA; 27114 MW; 885748E4A35FE7A8 CRC64;
MEHVFTPLEP LLPAGSLKFC LMILNQPLDK CFRHLWEKAL LRACADGGAN RLYDITGGER
ERFLPEFING DFDSIRPEVR EFYSVKGCEL LSTPDQDHTD FTKCLKVLQK KIEEKDLQVD
VIVTLGGLAG RFDQIMASVN TLFQATHITP LPVIMIQEES LIYLLQPGKH RLHVDTGMEG
SWCGLIPVGQ PCDHVTTTGL KWNLTNDVLG FGTLVSTSNT YDGSGVVTVE TSHPLLWTMA
IKN
//
