(data stored in ACNUC7421 zone)

SWISSPROT: THIL_ECO57

ID   THIL_ECO57              Reviewed;         325 AA.
AC   Q8XE87; Q7AH12;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   08-MAY-2019, entry version 107.
DE   RecName: Full=Thiamine-monophosphate kinase {ECO:0000255|HAMAP-Rule:MF_02128};
DE            Short=TMP kinase {ECO:0000255|HAMAP-Rule:MF_02128};
DE            Short=Thiamine-phosphate kinase {ECO:0000255|HAMAP-Rule:MF_02128};
DE            EC=2.7.4.16 {ECO:0000255|HAMAP-Rule:MF_02128};
GN   Name=thiL {ECO:0000255|HAMAP-Rule:MF_02128};
GN   OrderedLocusNames=Z0519, ECs0470;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of thiamine-
CC       monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the
CC       active form of vitamin B1. {ECO:0000255|HAMAP-Rule:MF_02128}.
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:0000255|HAMAP-Rule:MF_02128};
CC   -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis;
CC       thiamine diphosphate from thiamine phosphate: step 1/1.
CC       {ECO:0000255|HAMAP-Rule:MF_02128}.
CC   -!- MISCELLANEOUS: Reaction mechanism of ThiL seems to utilize a
CC       direct, inline transfer of the gamma-phosphate of ATP to TMP
CC       rather than a phosphorylated enzyme intermediate.
CC       {ECO:0000255|HAMAP-Rule:MF_02128}.
CC   -!- SIMILARITY: Belongs to the thiamine-monophosphate kinase family.
CC       {ECO:0000255|HAMAP-Rule:MF_02128}.
DR   EMBL; AE005174; AAG54766.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB33893.1; -; Genomic_DNA.
DR   PIR; B85538; B85538.
DR   PIR; F90687; F90687.
DR   RefSeq; NP_308497.1; NC_002695.1.
DR   RefSeq; WP_000742111.1; NZ_SDVX01000001.1.
DR   SMR; Q8XE87; -.
DR   STRING; 155864.EDL933_0485; -.
DR   EnsemblBacteria; AAG54766; AAG54766; Z0519.
DR   EnsemblBacteria; BAB33893; BAB33893; BAB33893.
DR   GeneID; 914572; -.
DR   KEGG; ece:Z0519; -.
DR   KEGG; ecs:ECs0470; -.
DR   PATRIC; fig|386585.9.peg.570; -.
DR   eggNOG; ENOG4105CG2; Bacteria.
DR   eggNOG; COG0611; LUCA.
DR   HOGENOM; HOG000228429; -.
DR   KO; K00946; -.
DR   BioCyc; ECOO157:THIL-MONOMER; -.
DR   UniPathway; UPA00060; UER00142.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; 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   3: Inferred from homology;
DR   PRODOM; Q8XE87.
DR   SWISS-2DPAGE; Q8XE87.
KW   ATP-binding; Complete proteome; Kinase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Reference proteome; Thiamine biosynthesis;
KW   Transferase.
FT   CHAIN         1    325       Thiamine-monophosphate kinase.
FT                                /FTId=PRO_0000096195.
FT   NP_BIND     121    122       ATP. {ECO:0000255|HAMAP-Rule:MF_02128}.
FT   METAL        30     30       Magnesium 3. {ECO:0000255|HAMAP-
FT                                Rule:MF_02128}.
FT   METAL        30     30       Magnesium 4; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_02128}.
FT   METAL        45     45       Magnesium 4. {ECO:0000255|HAMAP-
FT                                Rule:MF_02128}.
FT   METAL        46     46       Magnesium 1; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_02128}.
FT   METAL        47     47       Magnesium 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_02128}.
FT   METAL        47     47       Magnesium 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_02128}.
FT   METAL        75     75       Magnesium 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_02128}.
FT   METAL        75     75       Magnesium 3. {ECO:0000255|HAMAP-
FT                                Rule:MF_02128}.
FT   METAL        75     75       Magnesium 4. {ECO:0000255|HAMAP-
FT                                Rule:MF_02128}.
FT   METAL       122    122       Magnesium 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_02128}.
FT   METAL       212    212       Magnesium 3. {ECO:0000255|HAMAP-
FT                                Rule:MF_02128}.
FT   METAL       215    215       Magnesium 5. {ECO:0000255|HAMAP-
FT                                Rule:MF_02128}.
FT   BINDING      54     54       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_02128}.
FT   BINDING     146    146       ATP. {ECO:0000255|HAMAP-Rule:MF_02128}.
FT   BINDING     214    214       ATP. {ECO:0000255|HAMAP-Rule:MF_02128}.
FT   BINDING     263    263       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_02128}.
FT   BINDING     319    319       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_02128}.
SQ   SEQUENCE   325 AA;  35041 MW;  53C5DCF55050EC07 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
     FSDALSRHVV PEQALRWALS GGEDYELCFT VPELNRGALD VALGHLGVPF TCIGQMTADI
     EGLCFIRDGE PVTLDWKGYD HFATP
//

If you have problems or comments...

PBIL Back to PBIL home page