(data stored in SCRATCH zone)

SWISSPROT: Q3Z4Z2_SHISS

ID   Q3Z4Z2_SHISS            Unreviewed;       325 AA.
AC   Q3Z4Z2;
DT   27-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 83.
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:AAZ87170.1};
GN   OrderedLocusNames=SSON_0394 {ECO:0000313|EMBL:AAZ87170.1};
OS   Shigella sonnei (strain Ss046).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300269 {ECO:0000313|EMBL:AAZ87170.1, ECO:0000313|Proteomes:UP000002529};
RN   [1] {ECO:0000313|EMBL:AAZ87170.1, ECO:0000313|Proteomes:UP000002529}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ss046 {ECO:0000313|EMBL:AAZ87170.1,
RC   ECO:0000313|Proteomes:UP000002529};
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X.,
RA   Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S.,
RA   Nie H., Peng J., Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y.,
RA   Qiang B., Hou Y., Yu J., Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic
RT   agents of bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
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; CP000038; AAZ87170.1; -; Genomic_DNA.
DR   EnsemblBacteria; AAZ87170; AAZ87170; SSON_0394.
DR   KEGG; ssn:SSON_0394; -.
DR   HOGENOM; HOG000228429; -.
DR   KO; K00946; -.
DR   OMA; HFRRDWS; -.
DR   BioCyc; SSON300269:G1GL2-456-MONOMER; -.
DR   UniPathway; UPA00060; UER00142.
DR   Proteomes; UP000002529; 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; Q3Z4Z2.
DR   SWISS-2DPAGE; Q3Z4Z2.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_02128};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002529};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_02128, ECO:0000313|EMBL:AAZ87170.1};
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;  35105 MW;  9955DCEA7ACFFB8F 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 PVTFDWKGYD HFATP
//

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