CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003608
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Thiamine-monophosphate kinase 
Protein Synonyms/Alias
 TMP kinase; Thiamine-phosphate kinase 
Gene Name
 thiL 
Gene Synonyms/Alias
 b0417; JW0407 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
181RLQVADAKDADYLIKacetylation[1]
188KDADYLIKRHLRPSPacetylation[1]
Reference
 [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
 Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
 Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618
Functional Description
 Catalyzes the ATP-dependent phosphorylation of thiamine- monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the active form of vitamin B1. Can not use thiamine as substrate. Is highly specific for ATP as phosphate donor. 
Sequence Annotation
 NP_BIND 121 122 ATP (By similarity).
 METAL 30 30 Magnesium 3 (By similarity).
 METAL 30 30 Magnesium 4; via carbonyl oxygen (By
 METAL 45 45 Magnesium 4 (By similarity).
 METAL 46 46 Magnesium 1; via carbonyl oxygen (By
 METAL 47 47 Magnesium 1 (By similarity).
 METAL 47 47 Magnesium 2 (By similarity).
 METAL 75 75 Magnesium 2 (By similarity).
 METAL 75 75 Magnesium 3 (By similarity).
 METAL 75 75 Magnesium 4 (By similarity).
 METAL 122 122 Magnesium 1 (By similarity).
 METAL 212 212 Magnesium 3 (By similarity).
 METAL 215 215 Magnesium 5 (By similarity).
 BINDING 54 54 Substrate (By similarity).
 BINDING 146 146 ATP (By similarity).
 BINDING 214 214 ATP (By similarity).
 BINDING 263 263 Substrate (By similarity).
 BINDING 319 319 Substrate (By similarity).  
Keyword
 ATP-binding; Complete proteome; Kinase; Magnesium; Metal-binding; Nucleotide-binding; Reference proteome; Thiamine biosynthesis; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 325 AA 
Protein Sequence
MACGEFSLIA RYFDRVRSSR LDVELGIGDD CALLNIPEKQ TLAISTDTLV AGNHFLPDID 60
PADLAYKALA VNLSDLAAMG ADPAWLTLAL TLPDVDEAWL ESFSDSLFDL LNYYDMQLIG 120
GDTTRGPLSM TLGIHGFVPM GRALTRSGAK PGDWIYVTGT PGDSAAGLAI LQNRLQVADA 180
KDADYLIKRH LRPSPRILQG QALRDLANSA IDLSDGLISD LGHIVKASDC GARIDLALLP 240
FSDALSRHVE PEQALRWALS GGEDYELCFT VPELNRGALD VALGHLGVPF TCIGQMTADI 300
EGLCFIRDGE PVTLDWKGYD HFATP 325 
Gene Ontology
 GO:0005524; F:ATP binding; IEA:HAMAP.
 GO:0000287; F:magnesium ion binding; IEA:HAMAP.
 GO:0009030; F:thiamine-phosphate kinase activity; IDA:UniProtKB.
 GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW.
 GO:0009229; P:thiamine diphosphate biosynthetic process; IDA:UniProtKB. 
Interpro
 IPR010918; AIR_synth_C_dom.
 IPR000728; AIR_synth_N_dom.
 IPR016188; PurM_N-like.
 IPR006283; ThiL. 
Pfam
 PF00586; AIRS
 PF02769; AIRS_C 
SMART
  
PROSITE
  
PRINTS