J9N5G7 · THI4_FUSO4
- ProteinThiamine thiazole synthase
- Genesti35
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids320 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
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
- [ADP-thiazole synthase]-L-cysteine + glycine + NAD+ = [ADP-thiazole synthase]-dehydroalanine + ADP-5-ethyl-4-methylthiazole-2-carboxylate + 2 H+ + 3 H2O + nicotinamide
Cofactor
Note: Binds 1 Fe cation per subunit.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 82 | substrate | ||||
Sequence: C | ||||||
Binding site | 103-104 | substrate | ||||
Sequence: EA | ||||||
Binding site | 111 | substrate | ||||
Sequence: G | ||||||
Binding site | 176 | substrate | ||||
Sequence: V | ||||||
Binding site | 211 | substrate | ||||
Sequence: D | ||||||
Binding site | 226 | substrate | ||||
Sequence: H | ||||||
Binding site | 278 | substrate | ||||
Sequence: M | ||||||
Binding site | 288-290 | substrate | ||||
Sequence: RMG |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | nucleus | |
Molecular Function | ferrous iron binding | |
Molecular Function | pentosyltransferase activity | |
Biological Process | mitochondrial genome maintenance | |
Biological Process | thiamine 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
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Hypocreomycetidae > Hypocreales > Nectriaceae > Fusarium > Fusarium oxysporum species complex
Accessions
- Primary accessionJ9N5G7
Organism-specific databases
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000423475 | 1-320 | Thiamine thiazole synthase | |||
Sequence: MAPPAAVSPPSRSAELATSTKLPVMSKNINTKTVEEMLGQWDDFKFAPIRESQVSRAMTRRYFQDLDNYAESDIVIIGAGSCGLSAAYILGKKRPDLKIAIIEASVSPGGGAWLGGQLFSAMIMRKPADAFLREVGVPYEDEGNYVVVKHAALFTSTIMSKVLQMPNIKLFNATCVEDLITRPSEEGVRIAGVVTNWTLVSMHHDDQSCMDPNTINAPLIISTTGHDGPMGAFCVKRLVSMQRIEKLGGMRGLDMNLAEDAIVKGTREIVPGLIVGGMELSEVDGANRMGPTFGAMALSGLKAAEEALKIFDTRKKQNDL | ||||||
Modified residue | 209 | 2,3-didehydroalanine (Cys) | ||||
Sequence: C |
Post-translational modification
During the catalytic reaction, a sulfide is transferred from Cys-209 to a reaction intermediate, generating a dehydroalanine residue.
Interaction
Structure
Sequence
- Sequence statusComplete
- Length320
- Mass (Da)34,579
- Last updated2012-10-31 v1
- Checksum2287B18F266E2142
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AAXH01000627 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |