A0A8D5U0W7 · A0A8D5U0W7_9CREN
- ProteinThiamine thiazole synthase
- Genethi4
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids261 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
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.
Catalytic activity
- hydrogen sulfide + glycine + NAD+ = ADP-5-ethyl-4-methylthiazole-2-carboxylate + nicotinamide + 3 H2O + H+
Cofactor
Pathway
Cofactor biosynthesis; thiamine diphosphate biosynthesis.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 37 | NAD+ (UniProtKB | ChEBI); ligand shared between two adjacent protomers; in other chain | |||
Binding site | 56-57 | NAD+ (UniProtKB | ChEBI); ligand shared between two adjacent protomers; in other chain | |||
Binding site | 64 | NAD+ (UniProtKB | ChEBI); ligand shared between two adjacent protomers; in other chain | |||
Binding site | 128 | NAD+ (UniProtKB | ChEBI); ligand shared between two adjacent protomers; in other chain | |||
Binding site | 156-158 | NAD+ (UniProtKB | ChEBI); ligand shared between two adjacent protomers | |||
Binding site | 158 | Fe cation (UniProtKB | ChEBI); ligand shared between two adjacent protomers | |||
Binding site | 173 | Fe cation (UniProtKB | ChEBI); ligand shared between two adjacent protomers; in other chain | |||
Binding site | 223 | NAD+ (UniProtKB | ChEBI); ligand shared between two adjacent protomers; in other chain | |||
Binding site | 233 | glycine (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | iron ion binding | |
Molecular Function | isomerase activity | |
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
- Organism
- Strain
- Taxonomic lineageArchaea > Thermoproteota > Thermoprotei > Sulfolobales
Accessions
- Primary accessionA0A8D5U0W7
Proteomes
Interaction
Subunit
Homooctamer; tetramer of dimers.
Structure
Sequence
- Sequence statusComplete
- Length261
- Mass (Da)28,139
- Last updated2022-01-19 v1
- MD5 Checksum594EC2BD6691DFC4C51EA1573A8BC475
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AP024596 EMBL· GenBank· DDBJ | BCU67102.1 EMBL· GenBank· DDBJ | Genomic DNA |