(data stored in ACNUC7421 zone)

SWISSPROT: THIL_SALTY

ID   THIL_SALTY              Reviewed;         325 AA.
AC   P55881;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   11-DEC-2019, entry version 110.
DE   RecName: Full=Thiamine-monophosphate kinase;
DE            Short=TMP kinase;
DE            Short=Thiamine-phosphate kinase;
DE            EC=2.7.4.16;
GN   Name=thiL; OrderedLocusNames=STM0419;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   INDUCTION.
RC   STRAIN=LT2;
RX   PubMed=9188462; DOI=10.1074/jbc.272.25.15702;
RA   Webb E., Downs D.;
RT   "Characterization of thiL, encoding thiamin-monophosphate kinase, in
RT   Salmonella typhimurium.";
RL   J. Biol. Chem. 272:15702-15707(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
CC   -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of thiamine-
CC       monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the active
CC       form of vitamin B1. {ECO:0000269|PubMed:9188462}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + thiamine phosphate = ADP + thiamine diphosphate;
CC         Xref=Rhea:RHEA:15913, ChEBI:CHEBI:30616, ChEBI:CHEBI:37575,
CC         ChEBI:CHEBI:58937, ChEBI:CHEBI:456216; EC=2.7.4.16;
CC         Evidence={ECO:0000269|PubMed:9188462};
CC   -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis;
CC       thiamine diphosphate from thiamine phosphate: step 1/1.
CC   -!- INDUCTION: In contrast to other thiamine biosynthetic genes, thiL is
CC       not transcriptionally regulated by thiamine-pyrophosphate. Appears to
CC       be constitutively expressed. {ECO:0000269|PubMed:9188462}.
CC   -!- MISCELLANEOUS: Reaction mechanism of ThiL seems to utilize a direct,
CC       inline transfer of the gamma-phosphate of ATP to TMP rather than a
CC       phosphorylated enzyme intermediate. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the thiamine-monophosphate kinase family.
CC       {ECO:0000305}.
DR   EMBL; U74758; AAB37319.1; -; Genomic_DNA.
DR   EMBL; AE006468; AAL19373.1; -; Genomic_DNA.
DR   PIR; T47117; T47117.
DR   RefSeq; NP_459414.1; NC_003197.2.
DR   RefSeq; WP_000752138.1; NC_003197.2.
DR   SMR; P55881; -.
DR   PaxDb; P55881; -.
DR   PRIDE; P55881; -.
DR   EnsemblBacteria; AAL19373; AAL19373; STM0419.
DR   GeneID; 1251938; -.
DR   KEGG; stm:STM0419; -.
DR   PATRIC; fig|99287.12.peg.448; -.
DR   eggNOG; ENOG4105CG2; Bacteria.
DR   eggNOG; COG0611; LUCA.
DR   HOGENOM; HOG000228429; -.
DR   KO; K00946; -.
DR   OMA; HFRRDWS; -.
DR   PhylomeDB; P55881; -.
DR   BioCyc; SENT99287:STM0419-MONOMER; -.
DR   BRENDA; 2.7.4.16; 5542.
DR   UniPathway; UPA00060; UER00142.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009030; F:thiamine-phosphate kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd02194; ThiL; 1.
DR   Gene3D; 3.30.1330.10; -; 1.
DR   Gene3D; 3.90.650.10; -; 1.
DR   HAMAP; MF_02128; TMP_kinase; 1.
DR   InterPro; IPR010918; PurM-like_C_dom.
DR   InterPro; IPR036676; PurM-like_C_sf.
DR   InterPro; IPR016188; PurM-like_N.
DR   InterPro; IPR036921; PurM-like_N_sf.
DR   InterPro; IPR006283; ThiL.
DR   PANTHER; PTHR30270; PTHR30270; 1.
DR   Pfam; PF00586; AIRS; 1.
DR   Pfam; PF02769; AIRS_C; 1.
DR   PIRSF; PIRSF005303; Thiam_monoph_kin; 1.
DR   SUPFAM; SSF55326; SSF55326; 1.
DR   SUPFAM; SSF56042; SSF56042; 1.
DR   TIGRFAMs; TIGR01379; thiL; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P55881.
DR   SWISS-2DPAGE; P55881.
KW   ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Reference proteome; Thiamine biosynthesis; Transferase.
FT   CHAIN           1..325
FT                   /note="Thiamine-monophosphate kinase"
FT                   /id="PRO_0000096198"
FT   NP_BIND         121..122
FT                   /note="ATP"
FT                   /evidence="ECO:0000250"
FT   METAL           30
FT                   /note="Magnesium 3"
FT                   /evidence="ECO:0000250"
FT   METAL           30
FT                   /note="Magnesium 4; via carbonyl oxygen"
FT                   /evidence="ECO:0000250"
FT   METAL           45
FT                   /note="Magnesium 4"
FT                   /evidence="ECO:0000250"
FT   METAL           46
FT                   /note="Magnesium 1; via carbonyl oxygen"
FT                   /evidence="ECO:0000250"
FT   METAL           47
FT                   /note="Magnesium 1"
FT                   /evidence="ECO:0000250"
FT   METAL           47
FT                   /note="Magnesium 2"
FT                   /evidence="ECO:0000250"
FT   METAL           75
FT                   /note="Magnesium 2"
FT                   /evidence="ECO:0000250"
FT   METAL           75
FT                   /note="Magnesium 3"
FT                   /evidence="ECO:0000250"
FT   METAL           75
FT                   /note="Magnesium 4"
FT                   /evidence="ECO:0000250"
FT   METAL           122
FT                   /note="Magnesium 1"
FT                   /evidence="ECO:0000250"
FT   METAL           212
FT                   /note="Magnesium 3"
FT                   /evidence="ECO:0000250"
FT   METAL           215
FT                   /note="Magnesium 5"
FT                   /evidence="ECO:0000250"
FT   BINDING         54
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         146
FT                   /note="ATP"
FT                   /evidence="ECO:0000250"
FT   BINDING         214
FT                   /note="ATP"
FT                   /evidence="ECO:0000250"
FT   BINDING         263
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         319
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   325 AA;  34986 MW;  BF60DEB90C42B7CC CRC64;
     MACGEFSLIA RYFDRVRSSR LDVETGIGDD CALLNIPEKQ TLAISTDTLV AGNHFLPDID
     PADLAYKALA VNLSDLAAMG ADPAWLTLAL TLPEVDEPWL EAFSDSLFAL LNYYDMQLIG
     GDTTRGPLSM TLGIHGYIPA GRALKRSGAK PGDWIYVTGT PGDSAAGLAV LQNRLQVSEE
     TDAHYLIQRH LRPTPRILHG QALRDIASAA IDLSDGLISD LGHIVKASGC GARVDVDALP
     KSDAMMRHVD DGQALRWALS GGEDYELCFT VPELNRGALD VAIGQLGVPF TCIGQMSADI
     EGLNFVRDGM PVTFDWKGYD HFATP
//

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