A0A3A9LK82 · A0A3A9LK82_MORCA

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.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

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 site28Mg2+ 4 (UniProtKB | ChEBI)
Binding site28Mg2+ 3 (UniProtKB | ChEBI)
Binding site45Mg2+ 1 (UniProtKB | ChEBI)
Binding site45Mg2+ 2 (UniProtKB | ChEBI)
Binding site52substrate
Binding site73Mg2+ 3 (UniProtKB | ChEBI)
Binding site73Mg2+ 4 (UniProtKB | ChEBI)
Binding site73Mg2+ 2 (UniProtKB | ChEBI)
Binding site121-122ATP (UniProtKB | ChEBI)
Binding site122Mg2+ 1 (UniProtKB | ChEBI)
Binding site147ATP (UniProtKB | ChEBI)
Binding site219Mg2+ 3 (UniProtKB | ChEBI)
Binding site221ATP (UniProtKB | ChEBI)
Binding site222Mg2+ 5 (UniProtKB | ChEBI)
Binding site269substrate
Binding site322substrate

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
      D6D77_07970

Organism names

Accessions

  • Primary accession
    A0A3A9LK82

Proteomes

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain26-139PurM-like N-terminal

Sequence similarities

Belongs to the thiamine-monophosphate kinase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    325
  • Mass (Da)
    34,391
  • Last updated
    2018-12-05 v1
  • Checksum
    1E185741DEF75592
MSEFSLIHTHFKHLTAPHQHTVLGIGDDCAISNIPPNSQLVSCVDTLVAGRHFVHETSPHAIAYKSVAVNLSDLASMGAMPYAILVGLSLPKSMANDDFCQAFAEGLAAACTPFGVELIGGDTTSSPILTISVTALGFVPHGQAITRQGACVGDVVCVSGTVGLASLALHGILDDLNGDGHANRPPESLPEKLRQAMQYPAPQVALGKRLIGFANSMIDISDGLGQDLGHILTASNVGAVIELDAIPSHALLDALPHAQKWQHQINGGDDYQLCLTMPSAKLDLFKTQNPDMPIYPIGQIVADKGLVFLHNKKEVDLLVKGWAHF

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
QZGP01000006
EMBL· GenBank· DDBJ
RKL87914.1
EMBL· GenBank· DDBJ
Genomic DNA

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.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp