E0NE46 · E0NE46_PEDAC
- ProteinL-lactate oxidase
- GenelctO
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids369 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score2/5
Function
Catalytic activity
- (S)-lactate + O2 = H2O2 + pyruvateThis reaction proceeds in the forward direction.
Cofactor
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 39 | glyoxylate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 92 | FMN (UniProtKB | ChEBI) | ||||
Sequence: P | ||||||
Binding site | 92-94 | FMN (UniProtKB | ChEBI) | ||||
Sequence: PAA | ||||||
Binding site | 94 | FMN (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 121 | FMN (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 143 | FMN (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 145 | glyoxylate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 171 | FMN (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 180 | glyoxylate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 240 | FMN (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 262 | FMN (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Active site | 264 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 264 | glyoxylate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 267 | glyoxylate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 295 | FMN (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 295-299 | FMN (UniProtKB | ChEBI) | ||||
Sequence: DSGVR | ||||||
Binding site | 297 | FMN (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 299 | FMN (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 318 | FMN (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 318-319 | FMN (UniProtKB | ChEBI) | ||||
Sequence: GR | ||||||
Binding site | 319 | FMN (UniProtKB | ChEBI) | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | FMN binding | |
Molecular Function | oxidoreductase activity |
Keywords
- Molecular function
- Ligand
Names & Taxonomy
Protein names
- Recommended nameL-lactate oxidase
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Lactobacillales > Lactobacillaceae > Pediococcus > Pediococcus acidilactici group
Accessions
- Primary accessionE0NE46
Proteomes
Interaction
Subunit
Homotetramer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 13-369 | FMN hydroxy acid dehydrogenase | ||||
Sequence: EEKIDILNLESLEKQAEEIIPAGGFGYIAGGSEDEWTLKQNRMAFHHRQIAPKALSGIEKPELNTEIFGIPLNTPVMMAPAAAQGLAHSQGEKDTARGLAAVGGLMAQSTYSSVSIAETAAAGGDAPQFFQLYMSKDWNFNESLLDEAKKANVKAIILTVDATVDGYREADIKNKFTFPLPMANLIKFSEGNGQGKGIEEIYASAAQNIRPEDVKRIADYTNLPVIVKGIQTPEDAIRAIDAGAAGIYVSNHGGRQLNGGPASFDVLEDIATAVNKQVPIIFDSGVRRGSDVFKALASGADLVALGRPVIYGLALGGAKGVQSVFEHLNHELEIVMQLAGTKTIEDVKNNSLLNIKY |
Sequence similarities
Belongs to the FMN-dependent alpha-hydroxy acid dehydrogenase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length369
- Mass (Da)39,592
- Last updated2010-11-02 v1
- ChecksumCE4671D56BCD26DE
Keywords
- Technical term