B3DQ79 · B3DQ79_BIFLD
- ProteinMultifunctional fusion protein
- GenethiE
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids917 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Catalyzes the synthesis of the hydroxymethylpyrimidine phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent reaction.
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+ = CO2 + diphosphate + thiamine phosphate
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 Mg2+ ion per subunit.
Note: Binds 1 [4Fe-4S] cluster per subunit. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
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 | 48-52 | 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine (UniProtKB | ChEBI) | ||||
Sequence: QLRAK | ||||||
Binding site | 84 | 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 85 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 109 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 128 | 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 157-159 | 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: STT | ||||||
Binding site | 160 | 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 196 | 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 216-217 | 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: VS | ||||||
Binding site | 487 | substrate | ||||
Sequence: N | ||||||
Binding site | 516 | substrate | ||||
Sequence: M | ||||||
Binding site | 545 | substrate | ||||
Sequence: Y | ||||||
Binding site | 581 | substrate | ||||
Sequence: H | ||||||
Binding site | 601-603 | substrate | ||||
Sequence: SRG | ||||||
Binding site | 642-645 | substrate | ||||
Sequence: DGLR | ||||||
Binding site | 681 | substrate | ||||
Sequence: E | ||||||
Binding site | 685 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 708 | substrate | ||||
Sequence: Y | ||||||
Binding site | 749 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 829 | [4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 832 | [4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 837 | [4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | 4 iron, 4 sulfur cluster binding | |
Molecular Function | carbon-carbon lyase activity | |
Molecular Function | magnesium ion binding | |
Molecular Function | thiamine-phosphate diphosphorylase activity | |
Molecular Function | zinc ion binding | |
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 nameMultifunctional fusion protein
Including 2 domains:
- Recommended namePhosphomethylpyrimidine synthase
- EC number
- Alternative names
- Recommended nameThiamine-phosphate synthase
- EC number
- Short namesTP synthase ; TPS
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Bifidobacteriales > Bifidobacteriaceae > Bifidobacterium
Accessions
- Primary accessionB3DQ79
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 19-219 | Thiamine phosphate synthase/TenI | ||||
Sequence: YFVVGPEDCKGRPLTDVVDQALHGGATFIQLRAKEADASELTDMARDIAQIIEDNEKSDSVAFVIDDRADVVWQARRKGIKVDGVHIGQTDMEPREARALLGDEAIVGLSAETESLVRLINELPDGCIDYIGAGPLHVSTTKPEASVGGNDGSGKTLDAAQINTICVASEFPVVVGGGVTAADMAMLADTKAAGWFVVSAI | ||||||
Region | 256-311 | Disordered | ||||
Sequence: PATDTQAAQEGAAKPGSEATEKKFTNAKDAKDAQKLAKQQRVDIAARGSKQRDKAH | ||||||
Compositional bias | 276-293 | Basic and acidic residues | ||||
Sequence: EKKFTNAKDAKDAQKLAK |
Sequence similarities
Belongs to the ThiC family.
Belongs to the thiamine-phosphate synthase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length917
- Mass (Da)100,355
- Last updated2008-07-22 v1
- Checksum00000DA28A98E1F6
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 276-293 | Basic and acidic residues | ||||
Sequence: EKKFTNAKDAKDAQKLAK |
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000605 EMBL· GenBank· DDBJ | ACD97578.1 EMBL· GenBank· DDBJ | Genomic DNA |