F8WQN2 · LOX_CHLRE
- ProteinL-lactate oxidase
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids384 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Catalyzes the oxidation of (S)-lactate (L-lactate) to pyruvate, with a reduction of O2 to H2O2. Also shows a low oxidase activity with glycolate in vitro. The very low glycolate oxidase activity indicates that this enzyme is unlikely to be involved in photorespiratory glycolate metabolism, a pathway in which the oxidation of glycolate is taken over by glycolate dehydrogenase (GlcD).
Catalytic activity
- (S)-lactate + O2 = H2O2 + pyruvateThis reaction proceeds in the forward direction.
Cofactor
Note: Binds 1 FMN per subunit.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
0.081 mM | (S)-lactate | |||||
1.244 mM | glycolate | |||||
0.29 μM | O2 |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
10.59 μmol/min/mg | with (S)-lactate as substrate | ||||
0.189 μmol/min/mg | with glycolate as substrate |
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 27 | pyruvate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 80-82 | FMN (UniProtKB | ChEBI) | ||||
Sequence: PMA | ||||||
Binding site | 109 | FMN (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 130 | FMN (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 132 | pyruvate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 158 | FMN (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 167 | pyruvate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 237 | FMN (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 259 | FMN (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Active site | 261 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 261 | pyruvate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 264 | pyruvate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 295-299 | FMN (UniProtKB | ChEBI) | ||||
Sequence: DGGVR | ||||||
Binding site | 319 | FMN (UniProtKB | ChEBI) | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | (S)-2-hydroxy-acid oxidase activity | |
Molecular Function | FMN binding | |
Biological Process | response to other organism |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameL-lactate oxidase
- EC number
- Short namesLOX
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Viridiplantae > Chlorophyta > core chlorophytes > Chlorophyceae > CS clade > Chlamydomonadales > Chlamydomonadaceae > Chlamydomonas
Accessions
- Primary accessionF8WQN2
- Secondary accessions
Proteomes
Genome annotation databases
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000454867 | 1-384 | L-lactate oxidase | |||
Sequence: MADLSFLNLEEVEEEAKKVMPKMAFDYYSTGSDTCYTVGENRSCFSRYLLLPRMLRNVSRVDTSHELFGIRSSMPVWVAPMAMHGLAHPGREVATCRAAAAAGVPFTFSTVATSSLQEIQETGHDNRIFQLYVIRNREVVRRWVTEAESRGFKALMVTVDAQRLGNREADARNKFTLPPGLALRNLEYLSSASTVQARDSQDGSGLMKLFTSEVDDSLTWEFIPWLRGVTKLPIIVKGLLSPADAELAVQYGVDGIVVSNHGGRQLDYAPSGLHMLPAVVAAVRGCGSSIPVLVDGGVRRGTDVIKALALGASGVLLGRPVLYGLAVGGQAGVERVLQLLRSEIELSMALAGCSSVQQIGPQLLLPAPSAGPAPPMPAAQLCKL |
Proteomic databases
Expression
Gene expression databases
Interaction
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-369 | FMN hydroxy acid dehydrogenase | ||||
Sequence: MADLSFLNLEEVEEEAKKVMPKMAFDYYSTGSDTCYTVGENRSCFSRYLLLPRMLRNVSRVDTSHELFGIRSSMPVWVAPMAMHGLAHPGREVATCRAAAAAGVPFTFSTVATSSLQEIQETGHDNRIFQLYVIRNREVVRRWVTEAESRGFKALMVTVDAQRLGNREADARNKFTLPPGLALRNLEYLSSASTVQARDSQDGSGLMKLFTSEVDDSLTWEFIPWLRGVTKLPIIVKGLLSPADAELAVQYGVDGIVVSNHGGRQLDYAPSGLHMLPAVVAAVRGCGSSIPVLVDGGVRRGTDVIKALALGASGVLLGRPVLYGLAVGGQAGVERVLQLLRSEIELSMALAGCSSVQQIGPQLLLPAPS |
Sequence similarities
Belongs to the FMN-dependent alpha-hydroxy acid dehydrogenase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length384
- Mass (Da)41,308
- Last updated2011-10-19 v1
- ChecksumAF5614C041DE19CB
Sequence caution
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB610509 EMBL· GenBank· DDBJ | BAK61668.1 EMBL· GenBank· DDBJ | mRNA | ||
DS496116 EMBL· GenBank· DDBJ | EDP06163.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
CM008964 EMBL· GenBank· DDBJ | PNW85092.1 EMBL· GenBank· DDBJ | Genomic DNA |