Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003973 | molecular_function | (S)-2-hydroxy-acid oxidase activity |
A | 0005777 | cellular_component | peroxisome |
A | 0009853 | biological_process | photorespiration |
A | 0009854 | biological_process | oxidative photosynthetic carbon pathway |
A | 0010181 | molecular_function | FMN binding |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0051707 | biological_process | response to other organism |
B | 0003973 | molecular_function | (S)-2-hydroxy-acid oxidase activity |
B | 0005777 | cellular_component | peroxisome |
B | 0009853 | biological_process | photorespiration |
B | 0009854 | biological_process | oxidative photosynthetic carbon pathway |
B | 0010181 | molecular_function | FMN binding |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0051707 | biological_process | response to other organism |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE FMN A 370 |
Chain | Residue |
A | PHE24 |
A | THR155 |
A | LYS230 |
A | SER252 |
A | HIS254 |
A | ARG257 |
A | ASP285 |
A | GLY286 |
A | GLY287 |
A | ARG289 |
A | GLY308 |
A | TYR25 |
A | ARG309 |
A | ALA76 |
A | PRO77 |
A | ALA79 |
A | SER106 |
A | TRP108 |
A | GLN127 |
A | TYR129 |
Functional Information from PROSITE/UniProt
site_id | PS00557 |
Number of Residues | 7 |
Details | FMN_HYDROXY_ACID_DH_1 FMN-dependent alpha-hydroxy acid dehydrogenases active site. SNHGARQ |
Chain | Residue | Details |
A | SER252-GLN258 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | HIS254 | |
B | HIS254 | |
Chain | Residue | Details |
A | PHE24 | |
B | ARG257 | |
A | TYR129 | |
A | ARG164 | |
A | HIS254 | |
A | ARG257 | |
B | PHE24 | |
B | TYR129 | |
B | ARG164 | |
B | HIS254 | |
Chain | Residue | Details |
A | PRO77 | |
B | THR155 | |
B | LYS230 | |
B | SER252 | |
B | ASP285 | |
B | GLY308 | |
A | GLN127 | |
A | THR155 | |
A | LYS230 | |
A | SER252 | |
A | ASP285 | |
A | GLY308 | |
B | PRO77 | |
B | GLN127 | |
Chain | Residue | Details |
A | SER106 | |
B | SER106 | |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | SITE: Involved in determining the substrate specificity of glycolate oxidase => ECO:0000305|PubMed:7705356 |
Chain | Residue | Details |
A | TRP108 | |
B | TRP108 | |
Chain | Residue | Details |
A | MET1 | |
B | MET1 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1gox |
Chain | Residue | Details |
A | HIS254 | |
A | ARG257 | |
A | TYR129 | |
A | ASP157 | |
site_id | CSA2 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1gox |
Chain | Residue | Details |
B | HIS254 | |
B | ARG257 | |
B | TYR129 | |
B | ASP157 | |
site_id | MCSA1 |
Number of Residues | 5 |
Details | M-CSA 852 |
Chain | Residue | Details |
A | SER106 | electrostatic stabiliser |
A | TYR129 | electrostatic stabiliser, modifies pKa |
A | THR155 | electrostatic stabiliser |
A | LYS230 | electrostatic stabiliser, enhance reactivity |
A | HIS254 | proton shuttle (general acid/base) |
site_id | MCSA2 |
Number of Residues | 5 |
Details | M-CSA 852 |
Chain | Residue | Details |
B | SER106 | electrostatic stabiliser |
B | TYR129 | electrostatic stabiliser, modifies pKa |
B | THR155 | electrostatic stabiliser |
B | LYS230 | electrostatic stabiliser, enhance reactivity |
B | HIS254 | proton shuttle (general acid/base) |