Q5ZV75 · THI5_LEGPH
- Protein4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase
- Genethi5
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids316 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Responsible for the formation of the pyrimidine heterocycle in the thiamine biosynthesis pathway (PubMed:33034117).
Catalyzes the formation of hydroxymethylpyrimidine phosphate (HMP-P) from histidine and pyridoxal phosphate (PLP) (Probable). The protein uses PLP and the active site histidine to form HMP-P, generating an inactive enzyme (By similarity).
The enzyme can only undergo a single turnover, which suggests it is a suicide enzyme (By similarity).
Catalyzes the formation of hydroxymethylpyrimidine phosphate (HMP-P) from histidine and pyridoxal phosphate (PLP) (Probable). The protein uses PLP and the active site histidine to form HMP-P, generating an inactive enzyme (By similarity).
The enzyme can only undergo a single turnover, which suggests it is a suicide enzyme (By similarity).
Catalytic activity
- 2 Fe3+ + 4 H2O + L-histidyl-[4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase] + N6-(pyridoxal phosphate)-L-lysyl-[4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase] = (2S)-2-amino-5-hydroxy-4-oxopentanoyl-[4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase] + 3-oxopropanoate + 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + 2 Fe2+ + 2 H+ + L-lysyl-[4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase]This reaction proceeds in the forward direction.
2 CHEBI:29034 + 4 CHEBI:15377 + RHEA-COMP:16894 + RHEA-COMP:16892 = RHEA-COMP:16895 + CHEBI:33190 + CHEBI:58354 + 2 CHEBI:29033 + 2 CHEBI:15378 + RHEA-COMP:16893
Cofactor
Pathway
Cofactor biosynthesis; thiamine diphosphate biosynthesis.
Features
Showing features for active site, binding site.
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | 4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase activity from histidine and PLP | |
Molecular Function | metal ion binding | |
Molecular Function | vitamin B6 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 name4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase
- EC number
- Short namesHMP-P synthase ; Hydroxymethylpyrimidine phosphate synthase
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Legionellales > Legionellaceae > Legionella
Accessions
- Primary accessionQ5ZV75
Proteomes
Phenotypes & Variants
Disruption phenotype
Growth auxotrophic for thiamine; growth partially restored by hydroxymethylpyrimidine (HMP).
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 70 | Decreases pyridoxal phosphate (PLP) binding. | ||||
Sequence: H → A | ||||||
Mutagenesis | 118 | Decreases catalytic activity. | ||||
Sequence: G → A | ||||||
Mutagenesis | 119 | Decreases catalytic activity. | ||||
Sequence: E → A | ||||||
Mutagenesis | 120 | Decreases catalytic activity. | ||||
Sequence: F → A |
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000452085 | 1-316 | 4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase | |||
Sequence: MAMSSLKSRVTLLLNWYTNPYHTPILVAQQLGFYSEEDIKLAILEPADPSDVTEIVGLGTVDFGVKAMIHTVAAKAKGYPVTSIGTLLDEPPTGLIALKSSGINSFQDIVGKRVGYIGEFGKKIIDDLASLAGIDPTSYKTVRIGMNVTDAIYRDVIDTGIGFINFQKVELEHLCGETVFLRIDQLAGLGCCCFCSIQFIVPEITLQQPELVKGFLRATQRGAAYTTEKPEEAYELLCQAKPQLRTPLYQKIFTRTLPFFSRTLINVDRDWDKVGRYTKHLKIIDEHFDISQCYTNRFLPDTPYSDLKPIACCLEN | ||||||
Modified residue | 66 | N6-(pyridoxal phosphate)lysine | ||||
Sequence: K |
Proteomic databases
Interaction
Structure
Family & Domains
Features
Showing features for motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 191-195 | CCCFC; essential for catalytic activity, may be the site of iron coordination | ||||
Sequence: CCCFC |
Sequence similarities
Belongs to the NMT1/THI5 family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length316
- Mass (Da)35,276
- Last updated2004-11-23 v1
- Checksum07A59B40553DA971
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE017354 EMBL· GenBank· DDBJ | AAU27647.1 EMBL· GenBank· DDBJ | Genomic DNA |