ID B9EBA3_MACCJ Unreviewed; 212 AA.
AC B9EBA3;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=thiamine diphosphokinase {ECO:0000256|ARBA:ARBA00013245};
DE EC=2.7.6.2 {ECO:0000256|ARBA:ARBA00013245};
GN OrderedLocusNames=MCCL_0807 {ECO:0000313|EMBL:BAH17514.1};
OS Macrococcus caseolyticus (strain JCSC5402).
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae; Macrococcus.
OX NCBI_TaxID=458233 {ECO:0000313|EMBL:BAH17514.1, ECO:0000313|Proteomes:UP000001383};
RN [1] {ECO:0000313|EMBL:BAH17514.1, ECO:0000313|Proteomes:UP000001383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCSC5402 {ECO:0000313|EMBL:BAH17514.1,
RC ECO:0000313|Proteomes:UP000001383};
RX PubMed=19074389; DOI=10.1128/JB.01058-08;
RA Baba T., Kuwahara-Arai K., Uchiyama I., Takeuchi F., Ito T., Hiramatsu K.;
RT "Complete genome sequence of Macrococcus caseolyticus strain JCSCS5402,
RT reflecting the ancestral genome of the human-pathogenic staphylococci.";
RL J. Bacteriol. 191:1180-1190(2009).
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DR EMBL; AP009484; BAH17514.1; -; Genomic_DNA.
DR RefSeq; WP_012656714.1; NC_011999.1.
DR AlphaFoldDB; B9EBA3; -.
DR STRING; 458233.MCCL_0807; -.
DR KEGG; mcl:MCCL_0807; -.
DR eggNOG; COG1564; Bacteria.
DR HOGENOM; CLU_044237_1_0_9; -.
DR OrthoDB; 9804377at2; -.
DR Proteomes; UP000001383; 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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000001383};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 140..205
FT /note="Thiamin pyrophosphokinase thiamin-binding"
FT /evidence="ECO:0000259|SMART:SM00983"
SQ SEQUENCE 212 AA; 23986 MW; C5B7814482E05ED5 CRC64;
MNLHILCTQL EVDESIFERY GSDDWIGVDY GALMLIDRNI RPIAAFGDFD SIDETEKLRI
ESIIDIDYLA AEKNETDLEV AMQYAKDLEY NKVFIHGATG GRLDHFLGNL QTLLHPEILL
STSEFHIVNA NNTIQVLTAG THIIEHEPGK KYISFIPVND GVTLTLEGFK YDVDRLEVSL
GITRTVSNEF AERRAQVTVE QGMVYCIQST EQ
//
