| IED ID | IndEnz0007000239 |
| Enzyme Type ID | catalase000239 |
| Protein Name |
Glycolate oxidase 1 GOX 1 OsGLO1 EC 1.1.3.15 Peroxisomal S -2-hydroxy-acid oxidase GLO1 Short chain alpha-hydroxy acid oxidase GLO1 |
| Gene Name | GLO1 GOX Os03g0786100 LOC_Os03g57220 OsJ_12861 |
| Organism | Oryza sativa subsp. japonica (Rice) |
| Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae Liliopsida Petrosaviidae commelinids Poales Poaceae BOP clade Oryzoideae Oryzeae Oryzinae Oryza Oryza sativa (Rice) Oryza sativa subsp. japonica (Rice) |
| Enzyme Sequence | MGEITNVMEYQAIAKQKLPKMIYDYYASGAEDEWTLKENREAFSRILFRPRILIDVSKIDMSATVLGFKISMPIMIAPSAMQKMAHPDGEYATARAASAAGTIMTLSSWATSSVEEVASTGPGIRFFQLYVYKDRNVVEQLVRRAERAGFKAIALTVDTPRLGRREADIKNRFVLPPYLTLKNFEGLDLAEMDKSNDSGLASYVAGQIDRTLSWKDVKWLQSITSLPILVKGVITAEDARLAVHSGAAGIIVSNHGARQLDYVPATISALEEVVTAAAGRIPVYLDGGVRRGTDVFKALALGAAGVFIGRPVVFALAAEGEAGVRNVLRMMREEFELTMALSGCTSLADITRAHIYTDADRLARPFPRL |
| Enzyme Length | 369 |
| Uniprot Accession Number | Q10CE4 |
| Absorption | |
| Active Site | ACT_SITE 255; /note=Proton acceptor; /evidence=ECO:0000250|UniProtKB:P05414 |
| Activity Regulation | ACTIVITY REGULATION: Competitively inhibited by oxalate. {ECO:0000269|PubMed:16595582}. |
| Binding Site | BINDING 25; /note=Glyoxylate; /evidence=ECO:0000250|UniProtKB:Q9UJM8; BINDING 107; /note=FMN; /evidence=ECO:0000250|UniProtKB:P05414; BINDING 130; /note=Glyoxylate; /evidence=ECO:0000250|UniProtKB:Q9UJM8; BINDING 156; /note=FMN; /evidence=ECO:0000250|UniProtKB:P05414; BINDING 165; /note=Glyoxylate; /evidence=ECO:0000250|UniProtKB:Q9UJM8; BINDING 231; /note=FMN; /evidence=ECO:0000250|UniProtKB:P05414; BINDING 253; /note=FMN; /evidence=ECO:0000250|UniProtKB:P05414; BINDING 255; /note=Glyoxylate; /evidence=ECO:0000250|UniProtKB:Q9UJM8; BINDING 258; /note=Glyoxylate; /evidence=ECO:0000250|UniProtKB:Q9UJM8 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=glycolate + O2 = glyoxylate + H2O2; Xref=Rhea:RHEA:25311, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:29805, ChEBI:CHEBI:36655; EC=1.1.3.15; Evidence={ECO:0000269|PubMed:16595582};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25312; Evidence={ECO:0000305|PubMed:16595582}; |
| DNA Binding | |
| EC Number | 1.1.3.15 |
| Enzyme Function | FUNCTION: Catalyzes the oxidation of glycolate to glyoxylate, with a reduction of O2 to H2O2 (PubMed:16595582). Is a key enzyme in photorespiration in plants (By similarity). To a lesser extent, is also able to oxidize glyoxylate to oxalate in vitro (PubMed:16595582). Can exert a strong regulation over photosynthesis, possibly through a feed-back inhibition on Rubisco activase (PubMed:19264754). Does not seem to play a role in oxalate accumulation (PubMed:16595582). {ECO:0000250|UniProtKB:A0A3L6E0R4, ECO:0000269|PubMed:16595582, ECO:0000269|PubMed:19264754}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Photosynthesis; photorespiration; glycine from 2-phosphoglycolate: step 2/3. {ECO:0000250|UniProtKB:A0A3L6E0R4}. |
| nucleotide Binding | NP_BIND 78..80; /note=FMN; /evidence=ECO:0000250|UniProtKB:P05414; NP_BIND 128..130; /note=FMN; /evidence=ECO:0000250|UniProtKB:P05414; NP_BIND 286..290; /note=FMN; /evidence=ECO:0000250|UniProtKB:P05414; NP_BIND 309..310; /note=FMN; /evidence=ECO:0000250|UniProtKB:P05414 |
| Features | Active site (1); Binding site (9); Chain (1); Domain (1); Motif (1); Nucleotide binding (4); Site (1) |
| Keywords | FMN;Flavoprotein;Glycolate pathway;Host-virus interaction;Oxidoreductase;Peroxisome;Photorespiration;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:17174956}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 367..369; /note=Microbody targeting signal; /evidence=ECO:0000255 |
| Gene Encoded By | |
| Mass | 40,384 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.4 mM for glycolate (at pH 8.0 and 30 degrees Celsius) {ECO:0000269|PubMed:16595582}; KM=4 mM for glyoxylate (at pH 8.0 and 30 degrees Celsius) {ECO:0000269|PubMed:16595582}; |
| Metal Binding | |
| Rhea ID | RHEA:25311; RHEA:25312 |
| Cross Reference Brenda | 1.1.3.15; |