THIN_BACSU
ID THIN_BACSU Reviewed; 214 AA.
AC O34664; Q799K8;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Thiamine pyrophosphokinase;
DE Short=TPK;
DE EC=2.7.6.2;
DE AltName: Full=Thiamine diphosphokinase;
GN Name=thiN; Synonyms=yloS; OrderedLocusNames=BSU15800;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9534248; DOI=10.1099/00221287-144-3-801;
RA Foulger D., Errington J.;
RT "A 28 kbp segment from the spoVM region of the Bacillus subtilis 168
RT genome.";
RL Microbiology 144:801-805(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP CHARACTERIZATION.
RX PubMed=15150256; DOI=10.1128/jb.186.11.3660-3662.2004;
RA Melnick J., Lis E., Park J.-H., Kinsland C., Mori H., Baba T., Perkins J.,
RA Schyns G., Vassieva O., Osterman A., Begley T.P.;
RT "Identification of the two missing bacterial genes involved in thiamine
RT salvage: thiamine pyrophosphokinase and thiamine kinase.";
RL J. Bacteriol. 186:3660-3662(2004).
CC -!- FUNCTION: Catalyzes the phosphorylation of thiamine to thiamine
CC pyrophosphate.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + thiamine = AMP + H(+) + thiamine diphosphate;
CC Xref=Rhea:RHEA:11576, ChEBI:CHEBI:15378, ChEBI:CHEBI:18385,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58937, ChEBI:CHEBI:456215; EC=2.7.6.2;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=20 uM for thiamine;
CC KM=1 mM for ATP;
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis;
CC thiamine diphosphate from thiamine: step 1/1.
CC -!- SIMILARITY: Belongs to the thiamine pyrophosphokinase family.
CC {ECO:0000305}.
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DR EMBL; Y13937; CAA74253.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13453.1; -; Genomic_DNA.
DR PIR; C69879; C69879.
DR RefSeq; NP_389462.1; NC_000964.3.
DR RefSeq; WP_003245470.1; NZ_JNCM01000035.1.
DR PDB; 3LM8; X-ray; 2.60 A; A/B/C/D=1-214.
DR PDBsum; 3LM8; -.
DR AlphaFoldDB; O34664; -.
DR SMR; O34664; -.
DR STRING; 224308.BSU15800; -.
DR PaxDb; O34664; -.
DR EnsemblBacteria; CAB13453; CAB13453; BSU_15800.
DR GeneID; 937714; -.
DR KEGG; bsu:BSU15800; -.
DR PATRIC; fig|224308.179.peg.1720; -.
DR eggNOG; COG1564; Bacteria.
DR InParanoid; O34664; -.
DR OMA; ITYCPEG; -.
DR PhylomeDB; O34664; -.
DR BioCyc; BSUB:BSU15800-MON; -.
DR BioCyc; MetaCyc:BSU15800-MON; -.
DR UniPathway; UPA00060; UER00597.
DR EvolutionaryTrace; O34664; -.
DR Proteomes; UP000001570; 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:UniProtKB-UniPathway.
DR GO; GO:0006772; P:thiamine metabolic process; IEA:InterPro.
DR CDD; cd07995; TPK; 1.
DR Gene3D; 3.40.50.10240; -; 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 Pfam; PF04265; TPK_B1_binding; 1.
DR Pfam; PF04263; TPK_catalytic; 1.
DR SMART; SM00983; TPK_B1_binding; 1.
DR SUPFAM; SSF63862; SSF63862; 1.
DR SUPFAM; SSF63999; SSF63999; 1.
DR TIGRFAMs; TIGR01378; thi_PPkinase; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..214
FT /note="Thiamine pyrophosphokinase"
FT /id="PRO_0000072516"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:3LM8"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:3LM8"
FT HELIX 19..21
FT /evidence="ECO:0007829|PDB:3LM8"
FT STRAND 26..31
FT /evidence="ECO:0007829|PDB:3LM8"
FT HELIX 33..41
FT /evidence="ECO:0007829|PDB:3LM8"
FT STRAND 46..50
FT /evidence="ECO:0007829|PDB:3LM8"
FT HELIX 57..66
FT /evidence="ECO:0007829|PDB:3LM8"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:3LM8"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:3LM8"
FT HELIX 81..92
FT /evidence="ECO:0007829|PDB:3LM8"
FT STRAND 95..101
FT /evidence="ECO:0007829|PDB:3LM8"
FT HELIX 107..122
FT /evidence="ECO:0007829|PDB:3LM8"
FT STRAND 126..131
FT /evidence="ECO:0007829|PDB:3LM8"
FT STRAND 134..139
FT /evidence="ECO:0007829|PDB:3LM8"
FT STRAND 141..147
FT /evidence="ECO:0007829|PDB:3LM8"
FT STRAND 154..159
FT /evidence="ECO:0007829|PDB:3LM8"
FT STRAND 164..174
FT /evidence="ECO:0007829|PDB:3LM8"
FT STRAND 176..181
FT /evidence="ECO:0007829|PDB:3LM8"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:3LM8"
FT STRAND 193..205
FT /evidence="ECO:0007829|PDB:3LM8"
FT STRAND 207..212
FT /evidence="ECO:0007829|PDB:3LM8"
SQ SEQUENCE 214 AA; 24099 MW; 77BBA150330F4679 CRC64;
MKTINIVAGG PKNLIPDLTG YTDEHTLWIG VDKGTVTLLD AGIIPVEAFG DFDSITEQER
RRIEKAAPAL HVYQAEKDQT DLDLALDWAL EKQPDIIQIF GITGGRADHF LGNIQLLYKG
VKTNIKIRLI DKQNHIQMFP PGEYDIEKDE NKRYISFIPF SEDIHELTLT GFKYPLNNCH
ITLGSTLCIS NELIHSRGTF SFAKGILIMI RSTD
