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 03-AUG-2022, entry version 118.
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}.
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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 AlphaFoldDB; P55881; -.
DR SMR; P55881; -.
DR STRING; 99287.STM0419; -.
DR PaxDb; P55881; -.
DR DNASU; 1251938; -.
DR EnsemblBacteria; AAL19373; AAL19373; STM0419.
DR GeneID; 1251938; -.
DR KEGG; stm:STM0419; -.
DR PATRIC; fig|99287.12.peg.448; -.
DR HOGENOM; CLU_046964_3_0_6; -.
DR OMA; HFRRDWS; -.
DR PhylomeDB; P55881; -.
DR BioCyc; SENT99287:STM0419-MON; -.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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;
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 BINDING 30
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 30
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 45
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 46
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 47
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 47
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 54
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 75
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 75
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 75
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 121..122
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 122
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 146
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 212
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 214
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 215
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="5"
FT /evidence="ECO:0000250"
FT BINDING 263
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 319
FT /ligand="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
