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Database: UniProt
Entry: E1QVM5_OLSUV
LinkDB: E1QVM5_OLSUV
Original site: E1QVM5_OLSUV 
ID   E1QVM5_OLSUV            Unreviewed;       459 AA.
AC   E1QVM5;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   RecName: Full=thiamine diphosphokinase {ECO:0000256|ARBA:ARBA00013245};
DE            EC=2.7.6.2 {ECO:0000256|ARBA:ARBA00013245};
GN   OrderedLocusNames=Olsu_1068 {ECO:0000313|EMBL:ADK68178.1};
OS   Olsenella uli (strain ATCC 49627 / DSM 7084 / CIP 109912 / JCM 12494 /
OS   NCIMB 702895 / VPI D76D-27C) (Lactobacillus uli).
OC   Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales; Atopobiaceae;
OC   Olsenella.
OX   NCBI_TaxID=633147 {ECO:0000313|EMBL:ADK68178.1, ECO:0000313|Proteomes:UP000000333};
RN   [1] {ECO:0000313|EMBL:ADK68178.1, ECO:0000313|Proteomes:UP000000333}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49627 / DSM 7084 / CIP 109912 / JCM 12494 / NCIMB 702895 /
RC   VPI D76D-27C {ECO:0000313|Proteomes:UP000000333};
RX   PubMed=21304694; DOI=10.4056/sigs.1082860;
RA   Goker M., Held B., Lucas S., Nolan M., Yasawong M., Glavina Del Rio T.,
RA   Tice H., Cheng J.F., Bruce D., Detter J.C., Tapia R., Han C., Goodwin L.,
RA   Pitluck S., Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A.,
RA   Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Rohde M., Sikorski J., Pukall R., Woyke T., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Lapidus A.;
RT   "Complete genome sequence of Olsenella uli type strain (VPI D76D-27C).";
RL   Stand. Genomic Sci. 3:76-84(2010).
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DR   EMBL; CP002106; ADK68178.1; -; Genomic_DNA.
DR   RefSeq; WP_013251930.1; NZ_JQCO01000001.1.
DR   AlphaFoldDB; E1QVM5; -.
DR   STRING; 633147.Olsu_1068; -.
DR   GeneID; 78512488; -.
DR   KEGG; ols:Olsu_1068; -.
DR   PATRIC; fig|633147.7.peg.476; -.
DR   eggNOG; COG0637; Bacteria.
DR   eggNOG; COG1564; Bacteria.
DR   HOGENOM; CLU_612290_0_0_11; -.
DR   Proteomes; UP000000333; 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; cd07505; HAD_BPGM-like; 1.
DR   CDD; cd07995; TPK; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   Gene3D; 3.40.50.10240; Thiamin pyrophosphokinase, catalytic domain; 1.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006439; HAD-SF_hydro_IA.
DR   InterPro; IPR041492; HAD_2.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR023198; PGP-like_dom2.
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; TIGR01509; HAD-SF-IA-v3; 1.
DR   NCBIfam; TIGR01378; thi_PPkinase; 1.
DR   PANTHER; PTHR41299; THIAMINE PYROPHOSPHOKINASE; 1.
DR   PANTHER; PTHR41299:SF1; THIAMINE PYROPHOSPHOKINASE; 1.
DR   Pfam; PF13419; HAD_2; 1.
DR   Pfam; PF04265; TPK_B1_binding; 1.
DR   Pfam; PF04263; TPK_catalytic; 1.
DR   SFLD; SFLDG01129; C1.5:_HAD__Beta-PGM__Phosphata; 1.
DR   SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR   SMART; SM00983; TPK_B1_binding; 1.
DR   SUPFAM; SSF56784; HAD-like; 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:ADK68178.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000333};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          396..454
FT                   /note="Thiamin pyrophosphokinase thiamin-binding"
FT                   /evidence="ECO:0000259|SMART:SM00983"
SQ   SEQUENCE   459 AA;  49069 MW;  88531E85DA41A8A1 CRC64;
     MPIKAAIFDC DGTLVDSMPL WHDVTVELLR RHHVADAEEA FVRTESLPMV EMCHAFHDEW
     GVEAEGEELV RELVDMVREG YRSRVSLLPG CRAFLDELAS AGVRMVVASS TAPEELSVAL
     SAQGVDGYFE RVFSTGGPIR SKDYPDIWEL VLDYLGTDPA DTWVFEDAPF GMRTARSVGA
     NTVCLFSPHG DRDLAACERY ADILVHSYHE LSLALLDDYA RPPQASPSAH PRLAPLRVLV
     VGASPERPSS ALLRSLAAST DYVIAADAGA DALRSCGIAP DVFCGDADSA TGESAAWARS
     VARADIEFPS EKYATDLALA ISCARHEAAR RNARLELTLT GVTGGRPDHA LAVVGQLARN
     ADASPRIVED GFECRLLSPS GTACWELGGA HVPAAGVEGT LFSAIPVAEG TMLSERGFKW
     ELDHRELPLL GDEGISNVVT SATASVECHA GAVAAFLLA
//
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