ID A0A067RJS6_ZOONE Unreviewed; 300 AA.
AC A0A067RJS6;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=thiamine diphosphokinase {ECO:0000256|ARBA:ARBA00013245};
DE EC=2.7.6.2 {ECO:0000256|ARBA:ARBA00013245};
GN ORFNames=L798_07160 {ECO:0000313|EMBL:KDR23258.1};
OS Zootermopsis nevadensis (Dampwood termite).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Polyneoptera; Dictyoptera; Blattodea; Blattoidea; Termitoidae;
OC Termopsidae; Zootermopsis.
OX NCBI_TaxID=136037 {ECO:0000313|EMBL:KDR23258.1, ECO:0000313|Proteomes:UP000027135};
RN [1] {ECO:0000313|EMBL:KDR23258.1, ECO:0000313|Proteomes:UP000027135}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Whole organism {ECO:0000313|EMBL:KDR23258.1};
RX PubMed=24845553; DOI=10.1038/ncomms4636;
RA Terrapon N., Li C., Robertson H.M., Ji L., Meng X., Booth W., Chen Z.,
RA Childers C.P., Glastad K.M., Gokhale K., Gowin J., Gronenberg W.,
RA Hermansen R.A., Hu H., Hunt B.G., Huylmans A.K., Khalil S.M.,
RA Mitchell R.D., Munoz-Torres M.C., Mustard J.A., Pan H., Reese J.T.,
RA Scharf M.E., Sun F., Vogel H., Xiao J., Yang W., Yang Z., Yang Z., Zhou J.,
RA Zhu J., Brent C.S., Elsik C.G., Goodisman M.A., Liberles D.A., Roe R.M.,
RA Vargo E.L., Vilcinskas A., Wang J., Bornberg-Bauer E., Korb J., Zhang G.,
RA Liebig J.;
RT "Molecular traces of alternative social organization in a termite genome.";
RL Nat. Commun. 5:3636-3636(2014).
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DR EMBL; KK852470; KDR23258.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A067RJS6; -.
DR STRING; 136037.A0A067RJS6; -.
DR EnsemblMetazoa; KDR23258; KDR23258; L798_07160.
DR eggNOG; KOG3153; Eukaryota.
DR InParanoid; A0A067RJS6; -.
DR OMA; HHLYMMT; -.
DR OrthoDB; 102116at2759; -.
DR Proteomes; UP000027135; Unassembled WGS sequence.
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; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:InterPro.
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 Gene3D; 2.60.120.320; Thiamin pyrophosphokinase, thiamin-binding domain; 1.
DR InterPro; IPR006282; Thi_PPkinase.
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 SMART; SM00983; TPK_B1_binding; 1.
DR SUPFAM; SSF63999; Thiamin pyrophosphokinase, catalytic domain; 1.
DR SUPFAM; SSF63862; Thiamin pyrophosphokinase, substrate-binding domain; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KDR23258.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000027135};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 220..289
FT /note="Thiamin pyrophosphokinase thiamin-binding"
FT /evidence="ECO:0000259|SMART:SM00983"
SQ SEQUENCE 300 AA; 33240 MW; 43FD21F58843F2DA CRC64;
MNTAIWVFIR TYLTHSKVRM LLRNAIKNGM YFFQVVLDIG THGMNAPPVV NHWNPHDILD
VGNVSFRFGL LVLNQPINIE RELMFSLWNR ASLRVTVDGG TNRWFRFLQG GNCVAPELIT
GDMDSIKQNV LTHFKREGSQ IIPTPNQNET DFTKALRHVH GHIISKNLQL DGIIAVCETS
GRLDQILANL NTLYKAKDIV GNVPVYQLAK NSLSWLLAAG SHQINVGDAT VKKGCWCSLV
ALGAGVERVT TTGLKWNLDD RVMEFGGTIS TSNTYSGDPV VTVKTSGSLV WSMGLCDDDT
//