ID   TPK1_CAEEL              Reviewed;         243 AA.
AC   P30636; Q5FC86; Q6R5A6;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 3.
DT   27-MAR-2024, entry version 140.
DE   RecName: Full=Thiamin pyrophosphokinase 1;
DE            EC=2.7.6.2;
DE   AltName: Full=Thiamine pyrophosphokinase 1;
DE            Short=TPK1;
GN   Name=tpk-1 {ECO:0000312|WormBase:ZK637.9};
GN   ORFNames=ZK637.9 {ECO:0000312|WormBase:ZK637.9};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND MUTAGENESIS OF CYS-67.
RX   PubMed=15514058; DOI=10.1534/genetics.104.028605;
RA   de Jong L., Meng Y., Dent J., Hekimi S.;
RT   "Thiamine pyrophosphate biosynthesis and transport in the nematode
RT   Caenorhabditis elegans.";
RL   Genetics 168:845-854(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=1538779; DOI=10.1038/356037a0;
RA   Sulston J., Du Z., Thomas K., Wilson R., Hillier L., Staden R.,
RA   Halloran N., Green P., Thierry-Mieg J., Qiu L., Dear S., Coulson A.,
RA   Craxton M., Durbin R., Berks M., Metzstein M., Hawkins T., Ainscough R.,
RA   Waterston R.;
RT   "The C. elegans genome sequencing project: a beginning.";
RL   Nature 356:37-41(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [4]
RP   MUTAGENESIS OF CYS-67.
RX   PubMed=24107417; DOI=10.18632/aging.100604;
RA   Khan M.H., Ligon M., Hussey L.R., Hufnal B., Farber R. II, Munkacsy E.,
RA   Rodriguez A., Dillow A., Kahlig E., Rea S.L.;
RT   "TAF-4 is required for the life extension of isp-1, clk-1 and tpk-1 Mit
RT   mutants.";
RL   Aging (Albany NY) 5:741-758(2013).
CC   -!- FUNCTION: Catalyzes the phosphorylation of thiamine to thiamine
CC       pyrophosphate. Functions cell non-autonomously.
CC       {ECO:0000269|PubMed:15514058}.
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   -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis;
CC       thiamine diphosphate from thiamine: step 1/1.
CC   -!- SIMILARITY: Belongs to the thiamine pyrophosphokinase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAS21678.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY513235; AAS21678.1; ALT_SEQ; mRNA.
DR   EMBL; BX284603; CAI46594.1; -; Genomic_DNA.
DR   PIR; S15797; S15797.
DR   RefSeq; NP_001023023.1; NM_001027852.1.
DR   RefSeq; NP_001023024.1; NM_001027853.1.
DR   AlphaFoldDB; P30636; -.
DR   SMR; P30636; -.
DR   STRING; 6239.ZK637.9b.1; -.
DR   EPD; P30636; -.
DR   PaxDb; 6239-ZK637-9b; -.
DR   PeptideAtlas; P30636; -.
DR   EnsemblMetazoa; ZK637.9.1; ZK637.9.1; WBGene00014027.
DR   GeneID; 176258; -.
DR   KEGG; cel:CELE_ZK637.9; -.
DR   UCSC; ZK637.9b; c. elegans.
DR   AGR; WB:WBGene00014027; -.
DR   WormBase; ZK637.9; CE37947; WBGene00014027; tpk-1.
DR   eggNOG; KOG3153; Eukaryota.
DR   GeneTree; ENSGT00390000016016; -.
DR   InParanoid; P30636; -.
DR   OMA; TDMCKAL; -.
DR   OrthoDB; 102116at2759; -.
DR   PhylomeDB; P30636; -.
DR   BRENDA; 2.7.6.2; 1045.
DR   Reactome; R-CEL-196819; Vitamin B1 (thiamin) metabolism.
DR   UniPathway; UPA00060; UER00597.
DR   PRO; PR:P30636; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00014027; Expressed in germ line (C elegans) and 4 other cell types or tissues.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030975; F:thiamine binding; IEA:InterPro.
DR   GO; GO:0004788; F:thiamine diphosphokinase activity; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006772; P:thiamine metabolic process; IEA:InterPro.
DR   CDD; cd07995; TPK; 1.
DR   Gene3D; 3.40.50.10240; Thiamin pyrophosphokinase, catalytic 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   1: Evidence at protein level;
KW   ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN           1..243
FT                   /note="Thiamin pyrophosphokinase 1"
FT                   /id="PRO_0000072646"
FT   MUTAGEN         67
FT                   /note="C->Y: In qm162; maternal-effect mutation. Partial
FT                   loss-of-function. Prolongs embryonic and postembryonic
FT                   development, increases lifespan, reduces brood size,
FT                   reduces the rate of pharyngeal pumping and increases the
FT                   defecation cycle rate. Animals appear slimmer and more
FT                   transparent. In response to a thiamine-depleted diet, the
FT                   pharyngeal pumping rate further reduces and animals
FT                   subsquently die. In the absence of food, animals die within
FT                   a few days as arrested L1 larvae and fail to resume
FT                   development when placed in the presence of food. No effect
FT                   on oxygen consumption rate. Reduces lifespan in aha-1,
FT                   ceh-18, hif-1, jun-1, nhr-105 or taf-4 RNAi mutant
FT                   background."
FT                   /evidence="ECO:0000269|PubMed:15514058"
FT   CONFLICT        146..160
FT                   /note="Missing (in Ref. 1; AAS21678)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   243 AA;  27314 MW;  2BA5401B76326678 CRC64;
     MSKKLKPFEI LEDSCASVCI WLNGEPTAIS NRAENLWNKA KYRVATDGAV NEILKRKSFV
     EWPHIICGDF DSINKQIDTK NAKVVHLPDQ DYTDLSKSVQ WCLEQKTLTS WEFENIVVLG
     GLNGRFDHTM STLSSLIRFV DSQTPVIVLD SRNLVLAVPT GDSNLDVNLE MTTKMCGIIP
     IVQKETIVSS IGLKYEMENL ALEFGKLIST SNEVTTSQVF LKSSSSLIFS IELENWVYKL
     DSL
//