Q58018 · THI4_METJA
- ProteinThiamine thiazole synthase
- Genethi4
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids267 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
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.
Catalytic activity
- hydrogen sulfide + glycine + NAD+ = ADP-5-ethyl-4-methylthiazole-2-carboxylate + nicotinamide + 3 H2O + H+
Cofactor
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.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 47 | NAD+ (UniProtKB | ChEBI); ligand shared between two adjacent protomers; in other chain | |||
Binding site | 66-67 | NAD+ (UniProtKB | ChEBI); ligand shared between two adjacent protomers; in other chain | |||
Binding site | 74 | NAD+ (UniProtKB | ChEBI); ligand shared between two adjacent protomers; in other chain | |||
Binding site | 138 | NAD+ (UniProtKB | ChEBI); ligand shared between two adjacent protomers; in other chain | |||
Binding site | 164-166 | NAD+ (UniProtKB | ChEBI); ligand shared between two adjacent protomers | |||
Binding site | 166 | Fe cation (UniProtKB | ChEBI); ligand shared between two adjacent protomers | |||
Binding site | 181 | Fe cation (UniProtKB | ChEBI); ligand shared between two adjacent protomers; in other chain | |||
Binding site | 184 | NAD+ (UniProtKB | ChEBI); ligand shared between two adjacent protomers; in other chain | |||
Binding site | 230 | NAD+ (UniProtKB | ChEBI); ligand shared between two adjacent protomers; in other chain | |||
Binding site | 240 | glycine (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | iron ion binding | |
Molecular Function | pentosyltransferase activity | |
Biological Process | thiamine biosynthetic process | |
Biological Process | thiamine diphosphate biosynthetic process | |
Biological Process | thiazole biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameThiamine thiazole synthase
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageArchaea > Euryarchaeota > Methanomada group > Methanococci > Methanococcales > Methanocaldococcaceae > Methanocaldococcus
Accessions
- Primary accessionQ58018
Proteomes
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Mutagenesis | 164 | Still 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.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_0000153947 | 1-267 | Thiamine thiazole synthase | ||
Proteomic databases
Interaction
Structure
Sequence
- Sequence statusComplete
- Length267
- Mass (Da)28,655
- Last updated2010-11-02 v3
- Checksum2F359B900C838251
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
L77117 EMBL· GenBank· DDBJ | AAB98592.1 EMBL· GenBank· DDBJ | Genomic DNA |