J9N5G7 · THI4_FUSO4

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 site82substrate
Binding site103-104substrate
Binding site111substrate
Binding site176substrate
Binding site211substrate
Binding site226substrate
Binding site278substrate
Binding site288-290substrate

GO annotations

AspectTerm
Cellular Componentcytosol
Cellular Componentnucleus
Molecular Functionferrous iron binding
Molecular Functionpentosyltransferase activity
Biological Processmitochondrial genome maintenance
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
    • Stress-inducible protein sti35
    • Thiazole biosynthetic enzyme

Gene names

    • Name
      sti35
    • ORF names
      FOXG_10428

Organism names

Accessions

  • Primary accession
    J9N5G7

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00004234751-320Thiamine thiazole synthase
Modified residue2092,3-didehydroalanine (Cys)

Post-translational modification

During the catalytic reaction, a sulfide is transferred from Cys-209 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
    320
  • Mass (Da)
    34,579
  • Last updated
    2012-10-31 v1
  • Checksum
    2287B18F266E2142
MAPPAAVSPPSRSAELATSTKLPVMSKNINTKTVEEMLGQWDDFKFAPIRESQVSRAMTRRYFQDLDNYAESDIVIIGAGSCGLSAAYILGKKRPDLKIAIIEASVSPGGGAWLGGQLFSAMIMRKPADAFLREVGVPYEDEGNYVVVKHAALFTSTIMSKVLQMPNIKLFNATCVEDLITRPSEEGVRIAGVVTNWTLVSMHHDDQSCMDPNTINAPLIISTTGHDGPMGAFCVKRLVSMQRIEKLGGMRGLDMNLAEDAIVKGTREIVPGLIVGGMELSEVDGANRMGPTFGAMALSGLKAAEEALKIFDTRKKQNDL

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AAXH01000627
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.

Genome annotation databases

Similar Proteins

Disclaimer

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