C0NSF3 · THI4_AJECG

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 site86substrate
Binding site107-108substrate
Binding site115substrate
Binding site183substrate
Binding site223substrate
Binding site238substrate
Binding site290substrate
Binding site300-302substrate

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
      HCBG_06083

Organism names

Accessions

  • Primary accession
    C0NSF3

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

Type
IDPosition(s)Description
ChainPRO_00004158691-334Thiamine thiazole synthase
Modified residue2212,3-didehydroalanine (Cys)

Post-translational modification

During the catalytic reaction, a sulfide is transferred from Cys-221 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
    334
  • Mass (Da)
    35,737
  • Last updated
    2012-02-22 v2
  • Checksum
    CF3265D89DEB0CA0
MSPPSATYDVVAAAATSVAKTNKPSTAHGSLTSTSTILDEFAGKWDDFSFGHIRESQVSRAMTRRYFEDLDTYAESDIVIVGAGSCGLSTAYVLGKARPDLKIAVIEASVSPGGGAWLGGQLFSAMVLRKPADRFLDDLGVPYEEEPSNPNMVVIKHAALFTSTLLSKVLSFPNIKLFNATCVEDLITRPAPAAGDGEGIRIAGVVTNWTLVTLHHDDHSCMDPNTINAPLVISTTGHDGPFGAFCAKRLVSMAAIEKLGGMRGLDMNSAEEAIVKNTREVTKGLIIGGMELSEIDGWHRMGPIFSAMMLSGVRAAEVALEVFEERKRECADKK

Sequence caution

The sequence EEH05819.1 differs from that shown. Reason: Erroneous initiation Extended N-terminus.

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
GG663370
EMBL· GenBank· DDBJ
EEH05819.1
EMBL· GenBank· DDBJ
Genomic DNA Different initiation

Similar Proteins

Disclaimer

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