ID H1PLH6_9FIRM Unreviewed; 210 AA.
AC H1PLH6;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=thiamine diphosphokinase {ECO:0000256|ARBA:ARBA00013245};
DE EC=2.7.6.2 {ECO:0000256|ARBA:ARBA00013245};
GN ORFNames=HMPREF0380_01034 {ECO:0000313|EMBL:EHO85309.1};
OS Eubacterium infirmum F0142.
OC Bacteria; Bacillota; Clostridia; Eubacteriales;
OC Eubacteriales Family XIII. Incertae Sedis.
OX NCBI_TaxID=883109 {ECO:0000313|EMBL:EHO85309.1, ECO:0000313|Proteomes:UP000004504};
RN [1] {ECO:0000313|EMBL:EHO85309.1, ECO:0000313|Proteomes:UP000004504}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0142 {ECO:0000313|EMBL:EHO85309.1,
RC ECO:0000313|Proteomes:UP000004504};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Ganesan A.,
RA Baranova O.V., Blanton J.M., Tanner A.C., Dewhirst F.E., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Chapman S.B., Gearin G., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Heiman D., Howarth C., Larimer J., Lui A.,
RA MacDonald P.J.P., McCowen C., Montmayeur A., Murphy C., Neiman D.,
RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P., Stolte C.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Eubacterium infirmum F0142.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; AGWI01000014; EHO85309.1; -; Genomic_DNA.
DR AlphaFoldDB; H1PLH6; -.
DR STRING; 883109.HMPREF0380_01034; -.
DR PATRIC; fig|883109.3.peg.1032; -.
DR eggNOG; COG1564; Bacteria.
DR HOGENOM; CLU_044237_1_1_9; -.
DR Proteomes; UP000004504; 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 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; PTHR41299; THIAMINE PYROPHOSPHOKINASE; 1.
DR PANTHER; PTHR41299:SF1; THIAMINE PYROPHOSPHOKINASE; 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:EHO85309.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000004504};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 135..204
FT /note="Thiamin pyrophosphokinase thiamin-binding"
FT /evidence="ECO:0000259|SMART:SM00983"
SQ SEQUENCE 210 AA; 23264 MW; B3368B3286541571 CRC64;
MKKTIIVTAY IDRLSTIKGL HNFDSCIAAD GGYLNANKIG LAPDVIIGDF DSSQLPKKSN
AEILALPMEK DFTDTEAALD LAIKRGSEHV VIIGGLGRRF DHTLANLGIL AKYYKKLSHL
AFMDGYNYVY MLSPGSYRLQ KKIYGTEYKY LGVSSYSDYC KNLSIKGCKY PLEDYTLPKV
TSLGASNEII SYDAEISFSK GEIIITHSND
//
