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Database: UniProt
Entry: A0A101FNL8_9BACT
LinkDB: A0A101FNL8_9BACT
Original site: A0A101FNL8_9BACT 
ID   A0A101FNL8_9BACT        Unreviewed;       235 AA.
AC   A0A101FNL8;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   13-SEP-2023, entry version 18.
DE   RecName: Full=thiamine diphosphokinase {ECO:0000256|ARBA:ARBA00013245};
DE            EC=2.7.6.2 {ECO:0000256|ARBA:ARBA00013245};
GN   ORFNames=XD68_0106 {ECO:0000313|EMBL:KUK40336.1};
OS   Synergistales bacterium 54_24.
OC   Bacteria; Synergistota; Synergistia; Synergistales.
OX   NCBI_TaxID=1635272 {ECO:0000313|EMBL:KUK40336.1, ECO:0000313|Proteomes:UP000054050};
RN   [1] {ECO:0000313|Proteomes:UP000054050}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA   Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA   Andersen G.L., Banfield J.F.;
RT   "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT   Other Microbial Community Members in Biogeochemical Transformations in Oil
RT   Reservoirs.";
RL   MBio 7:e01669-15(2015).
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:KUK40336.1}.
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DR   EMBL; LGFQ01000002; KUK40336.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A101FNL8; -.
DR   STRING; 1635272.XD68_0106; -.
DR   Proteomes; UP000054050; 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:KUK40336.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          161..227
FT                   /note="Thiamin pyrophosphokinase thiamin-binding"
FT                   /evidence="ECO:0000259|SMART:SM00983"
SQ   SEQUENCE   235 AA;  26142 MW;  7D2CBD92E4D8FE39 CRC64;
     MKRLSIPGID AHYKDEVPEI CVLLVAGGRE PQISWLQEAA KRHRVWAVDR GVESCMRAHV
     LPELVIGDSD SGSPKAWEWA RSVGAEVHKF PRDKDLTDLQ LALRQLASLG LPVTTLLCGG
     WGMRFDHAWS NLFSLIWASK YGIEPGCICD EKEVLFFLRD GDHVELEFDV VPKAISLLSL
     SPVAEGVTAD GVKWPLKDKT LFLDEPYAVS NVPLDERVAF GVKSGWLGVY CTWEA
//
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