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Database: UniProt
Entry: A8X3A0_CAEBR
LinkDB: A8X3A0_CAEBR
Original site: A8X3A0_CAEBR 
ID   A8X3A0_CAEBR            Unreviewed;       225 AA.
AC   A8X3A0;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   27-MAR-2024, entry version 89.
DE   RecName: Full=Thiamine pyrophosphokinase {ECO:0000256|PIRNR:PIRNR031057};
DE            EC=2.7.6.2 {ECO:0000256|PIRNR:PIRNR031057};
GN   Name=tpk-1 {ECO:0000313|WormBase:CBG06882};
GN   Synonyms=Cbr-tpk-1 {ECO:0000313|EMBL:CAP27110.1};
GN   ORFNames=CBG06882 {ECO:0000313|WormBase:CBG06882}, CBG_06882
GN   {ECO:0000313|EMBL:CAP27110.1};
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238 {ECO:0000313|EMBL:CAP27110.1, ECO:0000313|Proteomes:UP000008549};
RN   [1] {ECO:0000313|EMBL:CAP27110.1, ECO:0000313|Proteomes:UP000008549}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16 {ECO:0000313|EMBL:CAP27110.1,
RC   ECO:0000313|Proteomes:UP000008549};
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
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; HE601347; CAP27110.1; -; Genomic_DNA.
DR   RefSeq; XP_002642467.1; XM_002642421.1.
DR   AlphaFoldDB; A8X3A0; -.
DR   STRING; 6238.A8X3A0; -.
DR   EnsemblMetazoa; CBG06882.1; CBG06882.1; WBGene00029077.
DR   GeneID; 8584461; -.
DR   KEGG; cbr:CBG_06882; -.
DR   CTD; 8584461; -.
DR   WormBase; CBG06882; CBP15764; WBGene00029077; Cbr-tpk-1.
DR   eggNOG; KOG3153; Eukaryota.
DR   HOGENOM; CLU_044237_0_1_1; -.
DR   InParanoid; A8X3A0; -.
DR   OMA; TDMCKAL; -.
DR   OrthoDB; 102116at2759; -.
DR   UniPathway; UPA00060; UER00597.
DR   Proteomes; UP000008549; Unassembled WGS sequence.
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; 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   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:UP000008549};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR031057}.
FT   DOMAIN          148..214
FT                   /note="Thiamin pyrophosphokinase thiamin-binding"
FT                   /evidence="ECO:0000259|SMART:SM00983"
SQ   SEQUENCE   225 AA;  25023 MW;  93EC783D67D58A41 CRC64;
     MSTSVCIWLN GEPTAIGKRA ENLWNSAKYR VATDGAINAI LKRKESVEWP HVICGDFDSM
     EAGIDTRNAK LLHLPDQDHT DLTKTIQWCL EQLSENQWKF EGILVLGGLN GRFDHTMSTL
     STLIHFLKAM TPIIVVDAYN MVLALPQGTS EIHVELEKTS KMCGVIPITQ KETIVTSKGL
     KYEMANLPLA FGKLISTSNE VTINQISLQS TAPLIFTIEL IHNQC
//
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