TPK1_CAEEL
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 03-AUG-2022, entry version 132.
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};
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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 AlphaFoldDB; P30636; -.
DR SMR; P30636; -.
DR STRING; 6239.ZK637.9b; -.
DR EPD; P30636; -.
DR PaxDb; P30636; -.
DR PeptideAtlas; P30636; -.
DR EnsemblMetazoa; ZK637.9.1; ZK637.9.1; WBGene00014027.
DR GeneID; 176258; -.
DR UCSC; ZK637.9b; c. elegans.
DR CTD; 176258; -.
DR WormBase; ZK637.9; CE37947; WBGene00014027; tpk-1.
DR eggNOG; KOG3153; Eukaryota.
DR GeneTree; ENSGT00390000016016; -.
DR InParanoid; P30636; -.
DR OMA; HHLYMMT; -.
DR OrthoDB; 1428589at2759; -.
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 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; -; 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 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; SSF63862; SSF63862; 1.
DR SUPFAM; SSF63999; SSF63999; 1.
DR TIGRFAMs; TIGR01378; thi_PPkinase; 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, ceh-
FT 18, hif-1, jun-1, nhr-105 or taf-4 RNAi mutant 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
