A0A1L8I8R1 · A0A1L8I8R1_9BACI
- ProteinPantothenate synthetase
- GenepanC
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids298 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
Miscellaneous
The reaction proceeds by a bi uni uni bi ping pong mechanism.
Catalytic activity
- (R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H+
Pathway
Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 30-37 | ATP (UniProtKB | ChEBI) | ||||
Sequence: MGYLHDGH | ||||||
Active site | 37 | Proton donor | ||||
Sequence: H | ||||||
Binding site | 61 | (R)-pantoate (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 61 | beta-alanine (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 148-151 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GQKD | ||||||
Binding site | 154 | (R)-pantoate (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 177 | ATP (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 185-188 | ATP (UniProtKB | ChEBI) | ||||
Sequence: MSSR |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | ATP binding | |
Molecular Function | pantoate-beta-alanine ligase activity | |
Biological Process | pantothenate biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePantothenate synthetase
- EC number
- Short namesPS
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Bacillales > Bacillaceae
Accessions
- Primary accessionA0A1L8I8R1
Proteomes
Subcellular Location
Interaction
Subunit
Homodimer.
Structure
Sequence
- Sequence statusComplete
- Length298
- Mass (Da)33,268
- Last updated2017-03-15 v1
- ChecksumB9FC641CE81DFA3F