E3JV98 · THI4_PUCGT

Function

function

Involved in biosynthesis of the thiamine precursor thiazole. Catalyzes the conversion of NAD and glycine to adenosine diphosphate 5-(2-hydroxyethyl)-4-methylthiazole-2-carboxylic acid (ADT), an adenylated thiazole intermediate. The reaction includes an iron-dependent sulfide transfer from a conserved cysteine residue of the protein to a thiazole intermediate. The enzyme can only undergo a single turnover, which suggests it is a suicide enzyme. May have additional roles in adaptation to various stress conditions and in DNA damage tolerance.

Catalytic activity

Cofactor

Fe cation (UniProtKB | Rhea| CHEBI:24875 )

Note: Binds 1 Fe cation per subunit.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site89substrate
Binding site110-111substrate
Binding site118substrate
Binding site183substrate
Binding site221substrate
Binding site236substrate
Binding site288substrate
Binding site298-300substrate

GO annotations

AspectTerm
Cellular Componentcytosol
Cellular Componentnucleus
Molecular Functioniron ion binding
Molecular Functionpentosyltransferase activity
Biological Processthiamine biosynthetic process
Biological Processthiazole biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Thiamine thiazole synthase
  • EC number
  • Alternative names
    • Thiazole biosynthetic enzyme

Gene names

    • ORF names
      PGTG_01304

Organism names

Accessions

  • Primary accession
    E3JV98

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00004158791-336Thiamine thiazole synthase
Modified residue2192,3-didehydroalanine (Cys)

Post-translational modification

During the catalytic reaction, a sulfide is transferred from Cys-219 to a reaction intermediate, generating a dehydroalanine residue.

Interaction

Subunit

Homooctamer.

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Belongs to the THI4 family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    336
  • Mass (Da)
    35,723
  • Last updated
    2011-01-11 v1
  • Checksum
    BF7D75C19CE5E389
MSPPVATESMYKPTTIGTEAHDQALAAMKSNQAAPAKPVFKPEPAVNLEPIKFAPIKEHQVQRAMVRRYFQDMEERAISDVIIVGAGSAGLSCAYALGKARPDLKITILESNVAPGGGCWLGGQLMSAMVCRKPADKFLDEVGVPYEDEGNFVVVKHAALFTSTVLSKVLAMPNVKMFNATACEDLIIKPCPINPGVQRVAGCVTNWTLVSLNHDHQSCMDPSTITAPLVCSFAGHDGPFGAFCVKRIASAGLSEGLGDMRPLDMERAEDHIANKTREIVPGLIVGGMELSEFDGSARMGPTFGAMLLSGKRAAEVALQSLGRVKVEEGEVVGSAK

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
DS178264
EMBL· GenBank· DDBJ
EFP75973.1
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