ID D1VWU2_9BACT Unreviewed; 216 AA.
AC D1VWU2;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE SubName: Full=Thiamine diphosphokinase {ECO:0000313|EMBL:EFA98441.1};
DE EC=2.7.6.2 {ECO:0000313|EMBL:EFA98441.1};
GN ORFNames=HMPREF9019_2217 {ECO:0000313|EMBL:EFA98441.1};
OS Hoylesella timonensis CRIS 5C-B1.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Hoylesella.
OX NCBI_TaxID=679189 {ECO:0000313|EMBL:EFA98441.1, ECO:0000313|Proteomes:UP000004001};
RN [1] {ECO:0000313|EMBL:EFA98441.1, ECO:0000313|Proteomes:UP000004001}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CRIS 5C-B1 {ECO:0000313|EMBL:EFA98441.1,
RC ECO:0000313|Proteomes:UP000004001};
RA Durkin A.S., Madupu R., Torralba M., Methe B., Sutton G., Strausberg R.L.,
RA Nelson K.E.;
RT "Genome Sequence of Prevotella timonensis CRIS 5C-B1.";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
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:EFA98441.1}.
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DR EMBL; ADEF01000005; EFA98441.1; -; Genomic_DNA.
DR RefSeq; WP_008122098.1; NZ_ADEF01000005.1.
DR AlphaFoldDB; D1VWU2; -.
DR eggNOG; COG1564; Bacteria.
DR Proteomes; UP000004001; 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: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; IPR049442; Thi_PPkinase-like_C.
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; PF21275; Thi_PPkinase_C; 1.
DR Pfam; PF04263; TPK_catalytic; 1.
DR SUPFAM; SSF63999; Thiamin pyrophosphokinase, catalytic domain; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EFA98441.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000004001};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EFA98441.1}.
FT DOMAIN 30..129
FT /note="Thiamin pyrophosphokinase catalytic"
FT /evidence="ECO:0000259|Pfam:PF04263"
FT DOMAIN 142..210
FT /note="Thiamin pyrophosphokinase-like substrate-binding"
FT /evidence="ECO:0000259|Pfam:PF21275"
SQ SEQUENCE 216 AA; 24438 MW; FE536DD114D2D6E6 CRC64;
MNYQLINSST NFDVVVLASG DYPQHAVPTQ ILQQASRIVC CDSAIELLHP SLYNKVEAVV
GDGDSMSDAA KLQFHDVLHV EHEQADNDLT KATRYCVSRN YSRIVYLGAT GKREDHSLGN
ISLMLRYFQT YGVQPVMVTD YGTFVPCLGD CTFESFAKQQ VSIFNFSCHR IESEGLRWQS
HAYQSWWEGT LNEAEGESFS IQSDGDYLVY RTHEPK
//
