Q88Q83 · GLYOX_PSEPK
- ProteinGlycine oxidase
- GenethiO
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids365 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the oxidation of glycine, leading to glyoxyl imine and hydrogen peroxide as primary products; glyoxyl imine is used for the biosynthesis of the thiazole ring of thiamine. Otherwise, glyoxyl imine is spontaneously hydrolyzed in water to produce glyoxylate and ammonia. Can also use sarcosine (N-methylglycine) as substrate, and, to a lesser extent, N-ethylglycine and D-proline. Has no activity towards other amino-acids D-Asp, D-Glu, D-Gln, D-His, D-Leu, D-Lys, D-ornithine, D-Trp, D-Val, L-Ala, L-Asp, L-Glu, L-His, L-Leu, L-Lys, L-Met and L-Pro.
Catalytic activity
- glycine + H2O + O2 = glyoxylate + H2O2 + NH4+
Cofactor
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
2.43 mM | glycine | |||||
4.86 mM | sarcosine | |||||
31.7 mM | D-proline | |||||
7.68 mM | N-ethylglycine |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
0.15 μmol/min/mg | with glycine as substrate | ||||
0.17 μmol/min/mg | with sarcosine as substrate | ||||
0.13 μmol/min/mg | with D-proline as substrate | ||||
0.11 μmol/min/mg | with N-ethylglycine as substrate |
pH Dependence
Optimum pH is 8.5.
Temperature Dependence
Optimum temperature is 40 degrees Celsius.
Pathway
Cofactor biosynthesis; thiamine diphosphate biosynthesis.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 12-13 | FAD (UniProtKB | ChEBI) | ||||
Sequence: VI | ||||||
Binding site | 32-33 | FAD (UniProtKB | ChEBI) | ||||
Sequence: DQ | ||||||
Binding site | 40-41 | FAD (UniProtKB | ChEBI) | ||||
Sequence: SS | ||||||
Binding site | 45-47 | FAD (UniProtKB | ChEBI) | ||||
Sequence: GGI | ||||||
Binding site | 173 | FAD (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Binding site | 302 | substrate | ||||
Sequence: R | ||||||
Binding site | 327-333 | FAD (UniProtKB | ChEBI) | ||||
Sequence: HYRNGLV |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | FAD binding | |
Molecular Function | glycine oxidase activity | |
Biological Process | amino acid metabolic process | |
Biological Process | thiamine biosynthetic process | |
Biological Process | thiamine diphosphate biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameGlycine oxidase
- EC number
- Short namesGO
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Pseudomonadaceae > Pseudomonas
Accessions
- Primary accessionQ88Q83
Proteomes
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000439958 | 1-365 | Glycine oxidase | |||
Sequence: MSKQVVVVGGGVIGLLTAFNLAAKVGQVVVCDQGEVGRESSWAGGGIVSPLYPWRYSPAVTALAHWSQDFYPQLGERLFASTGVDPEVHTTGLYWLDLDDEAEALAWAAREQRPLSAVDISAAYDAVPVLGPGFKHAIYMAGVANVRNPRLVKSLKAALLALPNVSLREHCQITGFVQEKGRVTGVQTADGVLAADEVVLSAGAWSGDLLRTLGLELPVEPVKGQMILFKCAEDFLPSMVLAKGRYAIPRRDGHILVGSTLEHAGYDKTPTADALESLKASAVELLPELEGATVVAHWAGLRPGSPEGIPYIGPVPGHEGLWLNCGHYRNGLVLAPASCQLFTDLLTGAEPIIDPAPYAPEGRLG |
Proteomic databases
Interaction
Structure
Sequence
- Sequence statusComplete
- Length365
- Mass (Da)38,679
- Last updated2003-06-01 v1
- ChecksumEC0EC9C3A78B6B56
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE015451 EMBL· GenBank· DDBJ | AAN66238.1 EMBL· GenBank· DDBJ | Genomic DNA |