Q9UVF8 · THI4_UROFA
- ProteinThiamine thiazole synthase
- GeneTHI2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids338 (go to sequence)
- Protein existenceEvidence at transcript level
- 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 | 91 | substrate | ||||
Sequence: A | ||||||
Binding site | 112-113 | substrate | ||||
Sequence: ES | ||||||
Binding site | 120 | substrate | ||||
Sequence: G | ||||||
Binding site | 185 | substrate | ||||
Sequence: C | ||||||
Binding site | 223 | substrate | ||||
Sequence: D | ||||||
Binding site | 238 | substrate | ||||
Sequence: H | ||||||
Binding site | 290 | substrate | ||||
Sequence: M | ||||||
Binding site | 300-302 | substrate | ||||
Sequence: RMG |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | nucleus | |
Molecular Function | iron ion binding | |
Molecular Function | pentosyltransferase activity | |
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
- Organism
- Taxonomic lineageEukaryota > Fungi > Dikarya > Basidiomycota > Pucciniomycotina > Pucciniomycetes > Pucciniales > Pucciniaceae > Uromyces
Accessions
- Primary accessionQ9UVF8
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000034057 | 1-338 | Thiamine thiazole synthase | |||
Sequence: MSPVATESMYKPTTINQTAHQQAMDPLKSKQQSNATVNKPAFKPEPAVNLTPIKFAPIKEHQVQRAMVRRYFQDMEERAISDVIIVGAGSAGLSCAYALGTARPDLKITILESNVAPGGGCWLGGQLMSAMVCRKPADEFLDQVGVPYEDEGNFVVVKHAALFTSTVLSKVLAMPNVKMFNATACEDLIIKPCPINPGVQRIAGCVTNWTLVSLNHDHQSCMDPSTITAPLVCSFAGHDGPFGAFCVKRVASAGLSEGLGDMRPLDMERAEDHIANKTREILPGLIVGGMELSEFDGSARMGPTFGAMLLSGKRAAEVALQSLDRVKIEEGEVVGLAK | ||||||
Modified residue | 221 | 2,3-didehydroalanine (Cys) | ||||
Sequence: C |
Post-translational modification
During the catalytic reaction, a sulfide is transferred from Cys-221 to a reaction intermediate, generating a dehydroalanine residue.
Expression
Tissue specificity
Highly expressed in haustoria, and only in low amounts in intercellular hyphae. Found in the basal hyphae of the uredia, but not in the pedicels and only at very low levels in uredospores.
Interaction
Subunit
Homooctamer.
Structure
Family & Domains
Features
Showing features for compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-39 | Polar residues | ||||
Sequence: MSPVATESMYKPTTINQTAHQQAMDPLKSKQQSNATVNK | ||||||
Region | 1-43 | Disordered | ||||
Sequence: MSPVATESMYKPTTINQTAHQQAMDPLKSKQQSNATVNKPAFK |
Sequence similarities
Belongs to the THI4 family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length338
- Mass (Da)36,213
- Last updated2000-05-01 v1
- ChecksumC3F9611094861230
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-39 | Polar residues | ||||
Sequence: MSPVATESMYKPTTINQTAHQQAMDPLKSKQQSNATVNK |