Q58018 · THI4_METJA

Function

function

Involved in the biosynthesis of the thiazole moiety of thiamine. Catalyzes the conversion of NAD and glycine to adenosine diphosphate 5-(2-hydroxyethyl)-4-methylthiazole-2-carboxylate (ADT), an adenylated thiazole intermediate, using free sulfide as a source of sulfur.

Miscellaneous

Unlike THI4 from S.cerevisiae, Thi4 from M.jannaschii can catalyze multiple turnovers because the sulfide is not enzyme derived.

Caution

This protein was originally thought to have NAD-dependent ribose 1,5-bisphosphate isomerase activity but the recombinant protein was not active in vitro (PubMed:15375115, PubMed:26919468).
In contrast, another protein from M.jannaschii likely possesses this activity (MJ0122)

Catalytic activity

Cofactor

Fe2+ (UniProtKB | Rhea| CHEBI:29033 )

Note: Binds 1 Fe2+ ion per subunit. Other divalent metal cations can support activity.

Pathway

Cofactor biosynthesis; thiamine diphosphate biosynthesis.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site47NAD+ (UniProtKB | ChEBI); ligand shared between two adjacent protomers; in other chain
Binding site66-67NAD+ (UniProtKB | ChEBI); ligand shared between two adjacent protomers; in other chain
Binding site74NAD+ (UniProtKB | ChEBI); ligand shared between two adjacent protomers; in other chain
Binding site138NAD+ (UniProtKB | ChEBI); ligand shared between two adjacent protomers; in other chain
Binding site164-166NAD+ (UniProtKB | ChEBI); ligand shared between two adjacent protomers
Binding site166Fe cation (UniProtKB | ChEBI); ligand shared between two adjacent protomers
Binding site181Fe cation (UniProtKB | ChEBI); ligand shared between two adjacent protomers; in other chain
Binding site184NAD+ (UniProtKB | ChEBI); ligand shared between two adjacent protomers; in other chain
Binding site230NAD+ (UniProtKB | ChEBI); ligand shared between two adjacent protomers; in other chain
Binding site240glycine (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular Functioniron ion binding
Molecular Functionpentosyltransferase activity
Biological Processthiamine biosynthetic process
Biological Processthiamine diphosphate biosynthetic process
Biological Processthiazole biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Thiamine thiazole synthase
  • EC number

Gene names

    • Name
      thi4
    • Ordered locus names
      MJ0601

Organism names

Accessions

  • Primary accession
    Q58018

Proteomes

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis164Still requires free sulfide for ADT synthesis, showing that this cysteine cannot act as an enzyme-derived sulfur source for thiazole formation as in S.cerevisiae.

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001539471-267Thiamine thiazole synthase

Proteomic databases

Interaction

Subunit

Homooctamer; tetramer of dimers.

Protein-protein interaction databases

Family & Domains

Sequence similarities

Belongs to the THI4 family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    267
  • Mass (Da)
    28,655
  • Last updated
    2010-11-02 v3
  • Checksum
    2F359B900C838251
MVNLMNIKDIKLNADETKTTKAILKASFDMWLDIVEADVVIVGAGPSGLTCARYLAKEGFKVVVLERHLAFGGGTWGGGMGFPYIVVEEPADELLREVGIKLIDMGDGYYVADSVEVPAKLAVAAMDAGAKILTGIVVEDLILREDGVAGVVINSYAIERAGLHIDPLTIRSKVVVDATGHEASIVNILVKKNKLEADVPGEKSMWAEKGENALLRNTREVYPNLFVCGMAANASHGGYRMGAIFGGMYLSGKLCAELITEKLKNKE

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
L77117
EMBL· GenBank· DDBJ
AAB98592.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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