ID A0A075JUR9_9BACI Unreviewed; 217 AA.
AC A0A075JUR9;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=thiamine diphosphokinase {ECO:0000256|ARBA:ARBA00013245};
DE EC=2.7.6.2 {ECO:0000256|ARBA:ARBA00013245};
GN ORFNames=X953_12170 {ECO:0000313|EMBL:AIF43803.1};
OS Virgibacillus sp. SK37.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Virgibacillus.
OX NCBI_TaxID=403957 {ECO:0000313|EMBL:AIF43803.1, ECO:0000313|Proteomes:UP000027985};
RN [1] {ECO:0000313|EMBL:AIF43803.1, ECO:0000313|Proteomes:UP000027985}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK37 {ECO:0000313|EMBL:AIF43803.1,
RC ECO:0000313|Proteomes:UP000027985};
RA Phrommao E., Yongsawatdigul J., Rodtong S., Steele J.L.;
RT "Complete genome sequence of Virgibacillus sp. SK37, a moderately
RT halophilic bacterium isolated from Thai fish sauce fermentation.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP007161; AIF43803.1; -; Genomic_DNA.
DR RefSeq; WP_040955707.1; NZ_CP007161.1.
DR AlphaFoldDB; A0A075JUR9; -.
DR STRING; 403957.X953_12170; -.
DR KEGG; vir:X953_12170; -.
DR HOGENOM; CLU_044237_1_0_9; -.
DR OrthoDB; 9804377at2; -.
DR Proteomes; UP000027985; Chromosome.
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:AIF43803.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000027985};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 141..207
FT /note="Thiamin pyrophosphokinase thiamin-binding"
FT /evidence="ECO:0000259|SMART:SM00983"
SQ SEQUENCE 217 AA; 24622 MW; BEB06D27A301D526 CRC64;
MRTIAIIGNS PDTYPDLQIY KDDVNVWIGA DRGSIELIRQ EMPVDYAIGD FDSTTEEERV
IIKGYCTEFE EYPSEKNETD LELALLKAFS LQPQRILLFG VTGGRLDHEL VNIQLLYRIV
CNNIKGIIID KNNILELTMP GIHKISLNAY YPTVSFIPYT KIVKGLSLTG FYYPLTKQNI
TWGSTLCISN KLIGKNGTFS YEEGILLLVK SRDTIQK
//
