A0A4R2S0J6 · A0A4R2S0J6_9FIRM

  • Protein
    Multifunctional fusion protein
  • Gene
    thiE
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

Function

function

Catalyzes the ATP-dependent phosphorylation of thiamine-monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the active form of vitamin B1.
Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).

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

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

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: Binds 1 Mg2+ ion per subunit.

Pathway

Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine diphosphate from thiamine phosphate: step 1/1.
Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site44-484-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine (UniProtKB | ChEBI)
Binding site764-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine (UniProtKB | ChEBI)
Binding site77Mg2+ (UniProtKB | ChEBI)
Binding site96Mg2+ (UniProtKB | ChEBI)
Binding site1154-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine (UniProtKB | ChEBI)
Binding site141-1432-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate (UniProtKB | ChEBI)
Binding site1444-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine (UniProtKB | ChEBI)
Binding site1712-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate (UniProtKB | ChEBI)
Binding site191-1922-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate (UniProtKB | ChEBI)
Binding site300Mg2+ 4 (UniProtKB | ChEBI)
Binding site300Mg2+ 3 (UniProtKB | ChEBI)
Binding site315Mg2+ 4 (UniProtKB | ChEBI)
Binding site316Mg2+ 1 (UniProtKB | ChEBI)
Binding site317Mg2+ 1 (UniProtKB | ChEBI)
Binding site317Mg2+ 2 (UniProtKB | ChEBI)
Binding site324substrate
Binding site346Mg2+ 3 (UniProtKB | ChEBI)
Binding site346Mg2+ 4 (UniProtKB | ChEBI)
Binding site346Mg2+ 2 (UniProtKB | ChEBI)
Binding site376ATP (UniProtKB | ChEBI)
Binding site393-394ATP (UniProtKB | ChEBI)
Binding site394Mg2+ 1 (UniProtKB | ChEBI)
Binding site418ATP (UniProtKB | ChEBI)
Binding site496Mg2+ 3 (UniProtKB | ChEBI)
Binding site498ATP (UniProtKB | ChEBI)
Binding site499Mg2+ 5 (UniProtKB | ChEBI)
Binding site549substrate
Binding site610substrate

GO annotations

AspectTerm
Molecular FunctionATP binding
Molecular Functionmagnesium ion binding
Molecular Functionthiamine-phosphate diphosphorylase activity
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
    Multifunctional fusion protein

Including 2 domains:

  • Recommended name
    Thiamine-phosphate synthase
  • EC number
  • Short names
    TP synthase
    ; TPS
  • Alternative names
    • Thiamine-phosphate pyrophosphorylase
      (TMP pyrophosphorylase
      ; TMP-PPase
      )
  • Recommended name
    Thiamine-monophosphate kinase
  • EC number
  • Short names
    TMP kinase
    ; Thiamine-phosphate kinase

Gene names

    • Name
      thiE
    • Synonyms
      thiL
    • ORF names
      EDD73_101105

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • DSM 11170
  • Taxonomic lineage
    Bacteria > Bacillota > Clostridia > Eubacteriales > Heliobacteriaceae > Heliophilum

Accessions

  • Primary accession
    A0A4R2S0J6

Proteomes

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain15-194Thiamine phosphate synthase/TenI
Domain298-411PurM-like N-terminal
Domain422-587PurM-like C-terminal

Sequence similarities

Belongs to the thiamine-monophosphate kinase family.
Belongs to the thiamine-phosphate synthase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    615
  • Mass (Da)
    65,052
  • Last updated
    2019-07-31 v1
  • Checksum
    B01912F8636511A6
MKKPIFWPQRLPWTYLVTDRALCQGRPLTMIVEQALRGGVKVVQYREKTLPTREMIAEASQLKDLCERYGALFVVNDRIDVALAVAAPAIHLGQEDMPIKHARAILGDDVLIGISASSVEEAQIAERDGADYIGASAVFATPTKEEAPALGLAGLKAICQAVSVPVVAIGGLHLGNVSDVIEAGSAGVAVVSAIMAASDPEAAAQALVQQLEAYRYQEESQETLAVTEETNGSVTRTPLSAVGEFGLIARLQEAWEKGGRESTEGAIQGETLEANSHDDGAFQWFPSSPLWGLRLGIGDDAAVLDFPAGKRCLVTTDMLVEDVHFIWHPERIHLLGRKALAVNISDIAAMGGRPGWAFLSIGVPPHAAVEEVEELYAGMGAVAADYGVLLSGGDTICADKWILNITLIGVAKGEPITRGGGRPGDFILVTGTVGDSAIGLQELLRPHHEFPELAETSGVFFRDDASFLLARHFDPTPRVPEALLLAAHGGVTAMMDVSDGISSEVHHLCRASRCGAQIDLTALPISPAAQRWSQAKGESVLPFALTGGEDYELIFTASPAAVPGLMASIQAQTGTTVTVIGQLTEPEAGITAVHPDIDGGAPNYLPAKGFNHFLE

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
SLXT01000001
EMBL· GenBank· DDBJ
TCP68939.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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