A0A517LTF7 · A0A517LTF7_9BACT

  • Protein
    Thiamine-phosphate synthase
  • Gene
    thiE
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

function

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).

Caution

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

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: Binds 1 Mg2+ ion per subunit.

Pathway

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 site204-2084-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine (UniProtKB | ChEBI)
Binding site2364-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine (UniProtKB | ChEBI)
Binding site237Mg2+ (UniProtKB | ChEBI)
Binding site256Mg2+ (UniProtKB | ChEBI)
Binding site2754-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine (UniProtKB | ChEBI)
Binding site301-3032-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate (UniProtKB | ChEBI)
Binding site3044-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine (UniProtKB | ChEBI)
Binding site3312-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Functionmagnesium ion binding
Molecular Functionthiamine-phosphate diphosphorylase activity
Biological Processthiamine biosynthetic process
Biological Processthiamine diphosphate biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

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

Gene names

    • Name
      thiE
    • ORF names
      EC9_00680

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • EC9
  • Taxonomic lineage
    Bacteria > Planctomycetota > Planctomycetia > Pirellulales > Pirellulaceae > Rosistilla

Accessions

  • Primary accession
    A0A517LTF7

Proteomes

Subcellular Location

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain36-158ThiD2
Domain175-354Thiamine phosphate synthase/TenI

Sequence similarities

Belongs to the thiamine-phosphate synthase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    380
  • Mass (Da)
    40,964
  • Last updated
    2019-10-16 v1
  • Checksum
    2DE809E1B7BE5E2D
MERCGFSGREKTEAIASVWEHKGMDGKESTPSGVWRILDASLNRASEGLRTIEEYARFVLGDPQLSEQLKQLRHQTATAAEGMPRLQLLAARDTPGDVGTAIETPTETERVDALAVAIAAAARVQQSLRCLEEYGKIVDSGIGRAFEACRYRSYTLFATLEQLSQRRDRLADCQLYVLVDGGDSIEAMTVTIAELAEAGADLIQLRDKRLNDRELYEHAAAAAATLRPSRCLFIVNDRPDIAAAVHADGVHVGQDELPATVVRQIIGPERLLGVSTHCVAQVEQAVSDGADYIGCGPTFPSGTKSFEAFPGTDFLRDAAATTTLPAFAIGGIGAENLAYVIEAGFSRVAVAGAITRSESPAAMVTELKQRLLRQDESTNR

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP036261
EMBL· GenBank· DDBJ
QDS85910.1
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.
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