A0A514LLX9 · A0A514LLX9_9BACI

Function

function

Catalyzes the ATP-dependent phosphorylation of thiamine-monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the active form of vitamin B1.

Miscellaneous

Reaction mechanism of ThiL seems to utilize a direct, inline transfer of the gamma-phosphate of ATP to TMP rather than a phosphorylated enzyme intermediate.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.

Catalytic activity

Pathway

Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine diphosphate from thiamine phosphate: step 1/1.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site27Mg2+ 3 (UniProtKB | ChEBI)
Binding site27Mg2+ 4 (UniProtKB | ChEBI)
Binding site44Mg2+ 1 (UniProtKB | ChEBI)
Binding site44Mg2+ 2 (UniProtKB | ChEBI)
Binding site51substrate
Binding site73Mg2+ 3 (UniProtKB | ChEBI)
Binding site73Mg2+ 4 (UniProtKB | ChEBI)
Binding site73Mg2+ 2 (UniProtKB | ChEBI)
Binding site103ATP (UniProtKB | ChEBI)
Binding site120-121ATP (UniProtKB | ChEBI)
Binding site121Mg2+ 1 (UniProtKB | ChEBI)
Binding site147ATP (UniProtKB | ChEBI)
Binding site216Mg2+ 3 (UniProtKB | ChEBI)
Binding site218ATP (UniProtKB | ChEBI)
Binding site219Mg2+ 5 (UniProtKB | ChEBI)
Binding site267substrate
Binding site324substrate

GO annotations

AspectTerm
Molecular FunctionATP binding
Molecular Functionmagnesium ion binding
Molecular Functionthiamine-phosphate kinase activity
Biological Processphosphorylation
Biological Processthiamine biosynthetic process
Biological Processthiamine diphosphate biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Thiamine-monophosphate kinase
  • EC number
  • Short names
    TMP kinase
    ; Thiamine-phosphate kinase

Gene names

    • Name
      thiL
    • ORF names
      EPH95_16220

Organism names

Accessions

  • Primary accession
    A0A514LLX9

Proteomes

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain25-139PurM-like N-terminal
Domain151-308PurM-like C-terminal

Sequence similarities

Belongs to the thiamine-monophosphate kinase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    327
  • Mass (Da)
    35,339
  • Last updated
    2019-10-16 v1
  • Checksum
    DE2F65C2E5FC28AE
MHEFDLIRQIDSFAADHEDVKVGIGDDAAVTSSHAHKDVISCVDTICEGIHFKRSTLHLSDIGYKALAVNLSDIAAMGGTPRYYLVSLAMSPEWKQEEILEIYRGMNDLAERYGVLLIGGDTVSAQHDLMISVTVLGEIEKSRSLLRSSAREGDVVFASGTLGDSRGGLDLLLSGGLTAPRTEQEHALVGVHQRPEPQLTLGQLLKESGCRIALNDISDGLSSESWELAEASRVCICLEEEKIPVSENATKLFGNETAYEYALTGGEDFQLVGTVAKSDWPAIASAAKEKGIRLSAIGSVTQEGAPQVLMQKNGERTAIKRAGYRHQ

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP035485
EMBL· GenBank· DDBJ
QDI92535.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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