ID Q55GR8_DICDI Unreviewed; 337 AA.
AC Q55GR8;
DT 24-MAY-2005, integrated into UniProtKB/TrEMBL.
DT 24-MAY-2005, sequence version 1.
DT 24-JAN-2024, entry version 101.
DE RecName: Full=thiamine diphosphokinase {ECO:0000256|ARBA:ARBA00013245};
DE EC=2.7.6.2 {ECO:0000256|ARBA:ARBA00013245};
GN ORFNames=DDB_G0267546 {ECO:0000313|EMBL:EAL73226.1};
OS Dictyostelium discoideum (Social amoeba).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689 {ECO:0000313|EMBL:EAL73226.1, ECO:0000313|Proteomes:UP000002195};
RN [1] {ECO:0000313|EMBL:EAL73226.1, ECO:0000313|Proteomes:UP000002195}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4 {ECO:0000313|EMBL:EAL73226.1,
RC ECO:0000313|Proteomes:UP000002195};
RX PubMed=15875012; DOI=10.1038/nature03481;
RG The Dictyostelium discoideum Sequencing Consortium;
RA Eichinger L., Pachebat J.A., Glockner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M., Spiegler S., Tivey A., Sugano S.,
RA White B., Walker D., Woodward J., Winckler T., Tanaka Y., Shaulsky G.,
RA Schleicher M., Weinstock G., Rosenthal A., Cox E.C., Chisholm R.L.,
RA Gibbs R., Loomis W.F., Platzer M., Kay R.R., Williams J., Dear P.H.,
RA Noegel A.A., Barrell B., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EAL73226.1}.
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DR EMBL; AAFI02000003; EAL73226.1; -; Genomic_DNA.
DR RefSeq; XP_647116.1; XM_642024.1.
DR AlphaFoldDB; Q55GR8; -.
DR SMR; Q55GR8; -.
DR STRING; 44689.Q55GR8; -.
DR PaxDb; 44689-DDB0189361; -.
DR EnsemblProtists; EAL73226; EAL73226; DDB_G0267546.
DR GeneID; 8615920; -.
DR KEGG; ddi:DDB_G0267546; -.
DR dictyBase; DDB_G0267546; -.
DR eggNOG; KOG3153; Eukaryota.
DR HOGENOM; CLU_044237_0_2_1; -.
DR InParanoid; Q55GR8; -.
DR PhylomeDB; Q55GR8; -.
DR Reactome; R-DDI-196819; Vitamin B1 (thiamin) metabolism.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0031012; C:extracellular matrix; HDA:dictyBase.
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; 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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000002195};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 247..329
FT /note="Thiamin pyrophosphokinase thiamin-binding"
FT /evidence="ECO:0000259|SMART:SM00983"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 60..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 337 AA; 37563 MW; 0655B11C8B262EA0 CRC64;
MEKQEEEVQQ QQQQQQQQQQ PDKNNKETIT WDVAEYGGYL FDKKLKAHNP LNHQMPLQYH
HSQSTPHIPS SLSTSSTTSI KKPSSSLSDD ESGGSSSSTP HSSNTPRKQF SFDDHCALIL
ANQKLPKKLV DYFWDKCSVR ICADGGANRL YSLGTKINQS SRWIPDYIKG DLDSLHEGVS
DFFSKKGSSI VLDSSQDTSD LQKCFELIID LEKGSGIKYR KIFILGGLGG SFSHEFANVN
TLFDHPGRKI ILASKDNLAW LLSSTYNHNI ICRSETKCSL IPLSSKASQV TTSGLKWNLV
KQSLNFGELI STSNVSLDNK VCVETSNPLI FIVDINP
//
