ID THIL_ECOLI Reviewed; 325 AA.
AC P0AGG0; O32380; P77785; Q2MC09;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 24-JAN-2024, entry version 127.
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=b0417, JW0407;
OS Escherichia coli (strain K12).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RA Iida A., Hayashi M., Fujio T., Teshiba S.;
RT "Molecular cloning, mapping, and sequencing of the thiL gene encoding
RT thiamine-monophosphate kinase in Escherichia coli K-12.";
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND ACTIVITY REGULATION.
RC STRAIN=K12;
RX PubMed=4567662; DOI=10.1093/oxfordjournals.jbchem.a129996;
RA Nishino H.;
RT "Biogenesis of cocarboxylase in Escherichia coli. Partial purification and
RT some properties of thiamine monophosphate kinase.";
RL J. Biochem. 72:1093-1100(1972).
RN [6]
RP IDENTIFICATION, AND FUNCTION.
RC STRAIN=K12;
RX PubMed=6284709; DOI=10.1128/jb.151.2.708-717.1982;
RA Imamura N., Nakayama H.;
RT "thiK and thiL loci of Escherichia coli.";
RL J. Bacteriol. 151:708-717(1982).
CC -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of thiamine-
CC monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the active
CC form of vitamin B1. Cannot use thiamine as substrate. Is highly
CC specific for ATP as phosphate donor. {ECO:0000269|PubMed:4567662,
CC ECO:0000269|PubMed:6284709}.
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:4567662};
CC -!- ACTIVITY REGULATION: Is markedly activated by the monovalent cations
CC K(+), NH(4)(+), and Rb(+). Is significantly inhibited by ADP, AMP, p-
CC chloromercuribenzoate, N-ethylmaleimide, pyrophosphate, and EDTA.
CC {ECO:0000269|PubMed:4567662}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.1 uM for thiamine-monophosphate {ECO:0000269|PubMed:4567662};
CC KM=270 uM for ATP {ECO:0000269|PubMed:4567662};
CC pH dependence:
CC Optimum pH is about 8.0. {ECO:0000269|PubMed:4567662};
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis;
CC thiamine diphosphate from thiamine phosphate: step 1/1.
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; D17333; BAA21778.1; -; Genomic_DNA.
DR EMBL; U82664; AAB40173.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73520.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76197.1; -; Genomic_DNA.
DR PIR; A64771; A64771.
DR RefSeq; NP_414951.1; NC_000913.3.
DR RefSeq; WP_000742109.1; NZ_SSZK01000009.1.
DR AlphaFoldDB; P0AGG0; -.
DR SMR; P0AGG0; -.
DR BioGRID; 4259339; 26.
DR BioGRID; 851709; 6.
DR IntAct; P0AGG0; 15.
DR STRING; 511145.b0417; -.
DR jPOST; P0AGG0; -.
DR PaxDb; 511145-b0417; -.
DR DNASU; 947387; -.
DR EnsemblBacteria; AAC73520; AAC73520; b0417.
DR GeneID; 947387; -.
DR KEGG; ecj:JW0407; -.
DR KEGG; eco:b0417; -.
DR PATRIC; fig|1411691.4.peg.1860; -.
DR EchoBASE; EB4149; -.
DR eggNOG; COG0611; Bacteria.
DR HOGENOM; CLU_046964_3_0_6; -.
DR InParanoid; P0AGG0; -.
DR OMA; HFRRDWS; -.
DR OrthoDB; 9802811at2; -.
DR PhylomeDB; P0AGG0; -.
DR BioCyc; EcoCyc:THI-P-KIN-MONOMER; -.
DR BioCyc; MetaCyc:THI-P-KIN-MONOMER; -.
DR UniPathway; UPA00060; UER00142.
DR PRO; PR:P0AGG0; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005524; F:ATP binding; IDA:EcoCyc.
DR GO; GO:0000287; F:magnesium ion binding; IDA:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IDA:EcoCyc.
DR GO; GO:0009030; F:thiamine-phosphate kinase activity; IDA:UniProtKB.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009228; P:thiamine biosynthetic process; IDA:EcoCyc.
DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IDA:UniProtKB.
DR CDD; cd02194; ThiL; 1.
DR Gene3D; 3.90.650.10; PurM-like C-terminal domain; 1.
DR Gene3D; 3.30.1330.10; PurM-like, N-terminal domain; 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-like.
DR NCBIfam; TIGR01379; thiL; 1.
DR PANTHER; PTHR30270; THIAMINE-MONOPHOSPHATE KINASE; 1.
DR PANTHER; PTHR30270:SF0; THIAMINE-MONOPHOSPHATE KINASE; 1.
DR Pfam; PF00586; AIRS; 1.
DR Pfam; PF02769; AIRS_C; 1.
DR PIRSF; PIRSF005303; Thiam_monoph_kin; 1.
DR SUPFAM; SSF56042; PurM C-terminal domain-like; 1.
DR SUPFAM; SSF55326; PurM N-terminal domain-like; 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_0000096194"
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"
FT CONFLICT 254
FT /note="A -> E (in Ref. 1; BAA21778)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 325 AA; 35071 MW; 9955DCE2D8CFFB8F CRC64;
MACGEFSLIA RYFDRVRSSR LDVELGIGDD CALLNIPEKQ TLAISTDTLV AGNHFLPDID
PADLAYKALA VNLSDLAAMG ADPAWLTLAL TLPDVDEAWL ESFSDSLFDL LNYYDMQLIG
GDTTRGPLSM TLGIHGFVPM GRALTRSGAK PGDWIYVTGT PGDSAAGLAI LQNRLQVADA
KDADYLIKRH LRPSPRILQG QALRDLANSA IDLSDGLISD LGHIVKASDC GARIDLALLP
FSDALSRHVE PEQALRWALS GGEDYELCFT VPELNRGALD VALGHLGVPF TCIGQMTADI
EGLCFIRDGE PVTLDWKGYD HFATP
//
