E3ZLZ6 · E3ZLZ6_LISSE
- ProteinThiamine-phosphate synthase
- GenethiE
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids214 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
Catalytic activity
- 2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 2 H+ = thiamine phosphate + CO2 + diphosphate
Cofactor
Note: Binds 1 Mg2+ ion per subunit.
Pathway
Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 37-41 | 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine (UniProtKB | ChEBI) | ||||
Sequence: QYREK | ||||||
Binding site | 73 | 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 74 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 93 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 112 | 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 139-141 | 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: TIS | ||||||
Binding site | 142 | 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 171 | 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 191-192 | 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: IS |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | magnesium ion binding | |
Molecular Function | thiamine-phosphate diphosphorylase activity | |
Biological Process | thiamine biosynthetic process | |
Biological Process | thiamine diphosphate biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameThiamine-phosphate synthase
- EC number
- Short namesTP synthase ; TPS
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Bacillales > Listeriaceae > Listeria
Accessions
- Primary accessionE3ZLZ6
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 7-194 | Thiamine phosphate synthase/TenI | ||||
Sequence: VYFIAGTQDIVRGNLPWVLEQALIAGITCFQYREKGARSLQSKDERKEMALTCQQLCQEYQVPFIVNDDVTLALEIGADGIHVGQDDEEILEVIRRVAGKMKIGLSVHSVSEAEEAVRLGAIDYIGVGPIFPTISKDDAEPVSGAGILEEIRRAGIAIPIVGIGGINEANCAEVLVAGADGVSVISAI |
Sequence similarities
Belongs to the thiamine-phosphate synthase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length214
- Mass (Da)22,887
- Last updated2011-02-08 v1
- Checksum3F5BF262065A964D
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
ADXJ01000180 EMBL· GenBank· DDBJ | EFS01357.1 EMBL· GenBank· DDBJ | Genomic DNA |