C4XIR5 · THI4_SOLM1
- ProteinThiamine thiazole synthase
- Genethi4
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids263 (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
- glycine + hydrogen sulfide + NAD+ = ADP-5-ethyl-4-methylthiazole-2-carboxylate + H+ + 3 H2O + nicotinamide
Cofactor
Pathway
Cofactor biosynthesis; thiamine diphosphate biosynthesis.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 36 | NAD+ (UniProtKB | ChEBI); ligand shared between two adjacent protomers; in other chain | ||||
Sequence: S | ||||||
Binding site | 55-56 | NAD+ (UniProtKB | ChEBI); ligand shared between two adjacent protomers; in other chain | ||||
Sequence: ER | ||||||
Binding site | 63 | NAD+ (UniProtKB | ChEBI); ligand shared between two adjacent protomers; in other chain | ||||
Sequence: G | ||||||
Binding site | 127 | NAD+ (UniProtKB | ChEBI); ligand shared between two adjacent protomers; in other chain | ||||
Sequence: V | ||||||
Binding site | 157-159 | NAD+ (UniProtKB | ChEBI); ligand shared between two adjacent protomers | ||||
Sequence: HVD | ||||||
Binding site | 159 | Fe cation (UniProtKB | ChEBI); ligand shared between two adjacent protomers | ||||
Sequence: D | ||||||
Binding site | 174 | Fe cation (UniProtKB | ChEBI); ligand shared between two adjacent protomers; in other chain | ||||
Sequence: H | ||||||
Binding site | 228 | NAD+ (UniProtKB | ChEBI); ligand shared between two adjacent protomers; in other chain | ||||
Sequence: M | ||||||
Binding site | 238 | glycine (UniProtKB | ChEBI) | ||||
Sequence: R |
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 lineageBacteria > Thermodesulfobacteriota > Desulfovibrionia > Desulfovibrionales > Desulfovibrionaceae > Solidesulfovibrio
Accessions
- Primary accessionC4XIR5
Proteomes
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_1000205004 | 1-263 | Thiamine thiazole synthase | |||
Sequence: MSLDERIITQAILETYFEKFKSSLDLDVAIVGGGPSGMTAARLLAADGFNVALFERKLSLGGGMWGGGMTFNMIVVQEESVHLLTDVGVPVKRYKDNYFTADAVAATTTLASAACLAGAKIFNCMSVEDVMLREENGVKRVTGIVINSSPVEIAGLHVDPVVLGSKYLVEATGHAVEVLQTLVRKNDVRLNTPSGGIEGEQSMWADTAEINTVKNTREIFPGLYVAGMAANASYGSYRMGPIFGGMLLSGEKVAADIAAKLKG |
Interaction
Structure
Sequence
- Sequence statusComplete
- Length263
- Mass (Da)27,873
- Last updated2009-07-28 v1
- ChecksumADA793304C972638
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AP010904 EMBL· GenBank· DDBJ | BAH76633.1 EMBL· GenBank· DDBJ | Genomic DNA |