ID A0A0K9GRY1_9BACI Unreviewed; 217 AA.
AC A0A0K9GRY1;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=thiamine diphosphokinase {ECO:0000256|ARBA:ARBA00013245};
DE EC=2.7.6.2 {ECO:0000256|ARBA:ARBA00013245};
GN ORFNames=AC625_07515 {ECO:0000313|EMBL:KMY49403.1};
OS Peribacillus loiseleuriae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Peribacillus.
OX NCBI_TaxID=1679170 {ECO:0000313|EMBL:KMY49403.1, ECO:0000313|Proteomes:UP000037146};
RN [1] {ECO:0000313|Proteomes:UP000037146}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FJAT-27997 {ECO:0000313|Proteomes:UP000037146};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA Shi H., Pan Z., Liu X.;
RT "Genome sequencing project for genomic taxonomy and phylogenomics of
RT Bacillus-like bacteria.";
RL Submitted (JUL-2015) 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:KMY49403.1}.
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DR EMBL; LFZW01000001; KMY49403.1; -; Genomic_DNA.
DR RefSeq; WP_049680735.1; NZ_LFZW01000001.1.
DR AlphaFoldDB; A0A0K9GRY1; -.
DR STRING; 1679170.AC625_07515; -.
DR PATRIC; fig|1679170.3.peg.1612; -.
DR OrthoDB; 9804377at2; -.
DR Proteomes; UP000037146; 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:KMY49403.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000037146};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 145..211
FT /note="Thiamin pyrophosphokinase thiamin-binding"
FT /evidence="ECO:0000259|SMART:SM00983"
SQ SEQUENCE 217 AA; 24206 MW; 3DAB006F543737A3 CRC64;
MIISIVAGGP VALLPDLNVY REKTSIWVGV DRGVYTLMHH DIVPDAAFGD FDSVTEAELA
DIKETLNHLE IYPTEKDETD LEIAFNWALS KHPEEIYVFG ATGGRMDHFI GNLQLLLKKP
LLEQKNNLNI SIVDKQNLIS FKTPGTYSLE AMNDKKYVSF LPISKEIKGI TLEGFKYPLT
NHVLPLGSTQ CISNELISQC GNFSFTDGIL MVIRSSD
//
