(data stored in ACNUC10821 zone)

SWISSPROT: C8U2A1_ECO10

ID   C8U2A1_ECO10            Unreviewed;       325 AA.
AC   C8U2A1;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 59.
DE   RecName: Full=Thiamine-monophosphate kinase {ECO:0000256|HAMAP-Rule:MF_02128};
DE            Short=TMP kinase {ECO:0000256|HAMAP-Rule:MF_02128};
DE            Short=Thiamine-phosphate kinase {ECO:0000256|HAMAP-Rule:MF_02128};
DE            EC=2.7.4.16 {ECO:0000256|HAMAP-Rule:MF_02128};
GN   Name=thiL {ECO:0000256|HAMAP-Rule:MF_02128,
GN   ECO:0000313|EMBL:BAI29259.1};
GN   OrderedLocusNames=ECO103_0391 {ECO:0000313|EMBL:BAI29259.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29259.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29259.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
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:0000256|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:0000256|HAMAP-Rule:MF_02128};
CC   -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis;
CC       thiamine diphosphate from thiamine phosphate: step 1/1.
CC       {ECO:0000256|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:0000256|HAMAP-Rule:MF_02128}.
CC   -!- SIMILARITY: Belongs to the thiamine-monophosphate kinase family.
CC       {ECO:0000256|HAMAP-Rule:MF_02128}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_02128}.
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DR   EMBL; AP010958; BAI29259.1; -; Genomic_DNA.
DR   RefSeq; WP_000742089.1; NC_013353.1.
DR   EnsemblBacteria; BAI29259; BAI29259; ECO103_0391.
DR   KEGG; eoh:ECO103_0391; -.
DR   HOGENOM; HOG000228429; -.
DR   KO; K00946; -.
DR   OMA; HFRRDWS; -.
DR   BioCyc; ECOL585395:ECO103_RS02050-MONOMER; -.
DR   UniPathway; UPA00060; UER00142.
DR   Proteomes; UP000000959; 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; C8U2A1.
DR   SWISS-2DPAGE; C8U2A1.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_02128};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_02128, ECO:0000313|EMBL:BAI29259.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_02128};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_02128};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02128};
KW   Thiamine biosynthesis {ECO:0000256|HAMAP-Rule:MF_02128};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_02128}.
FT   DOMAIN       29    138       AIRS. {ECO:0000259|Pfam:PF00586}.
FT   DOMAIN      150    299       AIRS_C. {ECO:0000259|Pfam:PF02769}.
FT   NP_BIND     121    122       ATP. {ECO:0000256|HAMAP-Rule:MF_02128}.
FT   METAL        30     30       Magnesium 3. {ECO:0000256|HAMAP-Rule:
FT                                MF_02128}.
FT   METAL        30     30       Magnesium 4; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_02128}.
FT   METAL        45     45       Magnesium 4. {ECO:0000256|HAMAP-Rule:
FT                                MF_02128}.
FT   METAL        46     46       Magnesium 1; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_02128}.
FT   METAL        47     47       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_02128}.
FT   METAL        47     47       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_02128}.
FT   METAL        75     75       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_02128}.
FT   METAL        75     75       Magnesium 3. {ECO:0000256|HAMAP-Rule:
FT                                MF_02128}.
FT   METAL        75     75       Magnesium 4. {ECO:0000256|HAMAP-Rule:
FT                                MF_02128}.
FT   METAL       122    122       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_02128}.
FT   METAL       212    212       Magnesium 3. {ECO:0000256|HAMAP-Rule:
FT                                MF_02128}.
FT   METAL       215    215       Magnesium 5. {ECO:0000256|HAMAP-Rule:
FT                                MF_02128}.
FT   BINDING      54     54       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02128}.
FT   BINDING     146    146       ATP. {ECO:0000256|HAMAP-Rule:MF_02128}.
FT   BINDING     214    214       ATP. {ECO:0000256|HAMAP-Rule:MF_02128}.
FT   BINDING     263    263       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02128}.
FT   BINDING     319    319       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02128}.
SQ   SEQUENCE   325 AA;  35145 MW;  93B8C4EA7D36638F CRC64;
     MACGEFSLIA RYFDRVRSSR LDVELGIGDD CALLNIPEKQ TLAISTDTLV AGNHFLHDID
     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 PVTFDWKGYD HFATP
//

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