P05414 · GOX_SPIOL
- ProteinGlycolate oxidase
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids369 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the oxidation of glycolate to glyoxylate, with a reduction of O2 to H2O2 (PubMed:1324737, PubMed:7705356).
Is a key enzyme in photorespiration in green plants (Probable). To a lesser extent, is also able to use L-lactate and 2-hydroxbyutanoate as substrate in vitro, but shows almost no activity with L-mandelate (PubMed:7705356).
Is a key enzyme in photorespiration in green plants (Probable). To a lesser extent, is also able to use L-lactate and 2-hydroxbyutanoate as substrate in vitro, but shows almost no activity with L-mandelate (PubMed:7705356).
Catalytic activity
- glycolate + O2 = glyoxylate + H2O2This reaction proceeds in the forward direction.
Cofactor
Note: Binds 1 FMN per subunit.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
0.2 mM | glycolate | 25 | ||||
1 mM | glycolate | |||||
11.5 mM | L-lactate | |||||
0.21 mM | O2 | |||||
3 mM | L-2-hydroxbyutanoate | |||||
58 mM | L-mandelate |
kcat is 20 sec-1 with glycolate as substrate. kcat is 11 sec-1 with L-lactate as substrate. kcat is 13.2 sec-1 with L-2-hydroxbyutanoate as substrate. kcat is 0.09 sec-1 with L-mandelate as substrate.
Pathway
Photosynthesis; photorespiration; glycine from 2-phosphoglycolate: step 2/3.
Features
Showing features for binding site, site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 24 | glyoxylate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 77-79 | FMN (UniProtKB | ChEBI) | ||||
Sequence: PTA | ||||||
Binding site | 106 | FMN (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Site | 108 | Involved in determining the substrate specificity of glycolate oxidase | ||||
Sequence: W | ||||||
Binding site | 127-129 | FMN (UniProtKB | ChEBI) | ||||
Sequence: QLY | ||||||
Binding site | 129 | glyoxylate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 155 | FMN (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 164 | glyoxylate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 230 | FMN (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 252 | FMN (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Active site | 254 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 254 | glyoxylate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 257 | glyoxylate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 285-289 | FMN (UniProtKB | ChEBI) | ||||
Sequence: DGGVR | ||||||
Binding site | 308-309 | FMN (UniProtKB | ChEBI) | ||||
Sequence: GR |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | peroxisome | |
Molecular Function | (S)-2-hydroxy-acid oxidase activity | |
Molecular Function | FMN binding | |
Biological Process | oxidative photosynthetic carbon pathway | |
Biological Process | response to other organism |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameGlycolate oxidase
- EC number
- Short namesGAO ; GOX
- Alternative names
Organism names
- Organism
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > Caryophyllales > Chenopodiaceae > Chenopodioideae > Anserineae > Spinacia
Accessions
- Primary accessionP05414
Proteomes
Subcellular Location
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 24 | 10-fold decrease in affinity for glycolate. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 108 | 100-fold decrease in affinity for glycolate and 500-fold decrease in activity. | ||||
Sequence: W → S |
PTM/Processing
Features
Showing features for modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 1 | N-acetylmethionine | ||||
Sequence: M | ||||||
Chain | PRO_0000206325 | 1-369 | Glycolate oxidase | |||
Sequence: MEITNVNEYEAIAKQKLPKMVYDYYASGAEDQWTLAENRNAFSRILFRPRILIDVTNIDMTTTILGFKISMPIMIAPTAMQKMAHPEGEYATARAASAAGTIMTLSSWATSSVEEVASTGPGIRFFQLYVYKDRNVVAQLVRRAERAGFKAIALTVDTPRLGRREADIKNRFVLPPFLTLKNFEGIDLGKMDKANDSGLSSYVAGQIDRSLSWKDVAWLQTITSLPILVKGVITAEDARLAVQHGAAGIIVSNHGARQLDYVPATIMALEEVVKAAQGRIPVFLDGGVRRGTDVFKALALGAAGVFIGRPVVFSLAAEGEAGVKKVLQMMRDEFELTMALSGCRSLKEISRSHIAADWDGPSSRAVARL |
Keywords
- PTM
PTM databases
Interaction
Subunit
Homotetramer.
Structure
Family & Domains
Features
Showing features for domain, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-359 | FMN hydroxy acid dehydrogenase | ||||
Sequence: MEITNVNEYEAIAKQKLPKMVYDYYASGAEDQWTLAENRNAFSRILFRPRILIDVTNIDMTTTILGFKISMPIMIAPTAMQKMAHPEGEYATARAASAAGTIMTLSSWATSSVEEVASTGPGIRFFQLYVYKDRNVVAQLVRRAERAGFKAIALTVDTPRLGRREADIKNRFVLPPFLTLKNFEGIDLGKMDKANDSGLSSYVAGQIDRSLSWKDVAWLQTITSLPILVKGVITAEDARLAVQHGAAGIIVSNHGARQLDYVPATIMALEEVVKAAQGRIPVFLDGGVRRGTDVFKALALGAAGVFIGRPVVFSLAAEGEAGVKKVLQMMRDEFELTMALSGCRSLKEISRSHIAADWD | ||||||
Motif | 367-369 | Microbody targeting signal | ||||
Sequence: ARL |
Sequence similarities
Belongs to the FMN-dependent alpha-hydroxy acid dehydrogenase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length369
- Mass (Da)40,286
- Last updated1988-11-01 v1
- Checksum892F1B3D0C1B48E0
Keywords
- Technical term