ID A0A098EJH6_9BACL Unreviewed; 222 AA.
AC A0A098EJH6;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=thiamine diphosphokinase {ECO:0000256|ARBA:ARBA00013245};
DE EC=2.7.6.2 {ECO:0000256|ARBA:ARBA00013245};
GN Name=thiN {ECO:0000313|EMBL:CEG22439.1};
GN ORFNames=BN1080_01368 {ECO:0000313|EMBL:CEG22439.1};
OS Planococcus massiliensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Planococcus.
OX NCBI_TaxID=1499687 {ECO:0000313|EMBL:CEG22439.1, ECO:0000313|Proteomes:UP000043699};
RN [1] {ECO:0000313|EMBL:CEG22439.1, ECO:0000313|Proteomes:UP000043699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ES2 {ECO:0000313|EMBL:CEG22439.1,
RC ECO:0000313|Proteomes:UP000043699};
RA Urmite Genomes Urmite Genomes;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CCXS01000001; CEG22439.1; -; Genomic_DNA.
DR RefSeq; WP_052651191.1; NZ_LR698965.1.
DR AlphaFoldDB; A0A098EJH6; -.
DR STRING; 1499687.BN1080_01368; -.
DR OrthoDB; 9804377at2; -.
DR Proteomes; UP000043699; 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:CEG22439.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000043699};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 141..206
FT /note="Thiamin pyrophosphokinase thiamin-binding"
FT /evidence="ECO:0000259|SMART:SM00983"
SQ SEQUENCE 222 AA; 24950 MW; EE554DA9837B77F0 CRC64;
MIVVVIAGGP RSEMPDFSEW KEAAFIGVDA GTVVLLDQGI RPIAAVGDFD SVTEEEMQRI
ETLFPALDRA AAEKDETDTE LALVKAMEFS PRQVIVTGVT GGRLDHYMSS LHAVYRMQQE
FPDTEFMLVN RQNRIRFLSP GSHRVQADKK YRYISFYPFA EAVEGFSLTH FKYEVADETL
PFGSTRFISN ELETEGIVAF SKGSCAMIES SDRADELEQR NK
//
