Q88Q83 · GLYOX_PSEPK

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

Cofactor

FAD (UniProtKB | Rhea| CHEBI:57692 )

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
2.43 mMglycine
4.86 mMsarcosine
31.7 mMD-proline
7.68 mMN-ethylglycine
Vmax pH TEMPERATURE[C] NOTES EVIDENCE
0.15 μmol/min/mgwith glycine as substrate
0.17 μmol/min/mgwith sarcosine as substrate
0.13 μmol/min/mgwith D-proline as substrate
0.11 μmol/min/mgwith 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.

TypeIDPosition(s)Description
Binding site12-13FAD (UniProtKB | ChEBI)
Binding site32-33FAD (UniProtKB | ChEBI)
Binding site40-41FAD (UniProtKB | ChEBI)
Binding site45-47FAD (UniProtKB | ChEBI)
Binding site173FAD (UniProtKB | ChEBI)
Binding site302substrate
Binding site327-333FAD (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular FunctionFAD binding
Molecular Functionglycine oxidase activity
Biological Processamino acid metabolic process
Biological Processthiamine biosynthetic process
Biological Processthiamine diphosphate biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Glycine oxidase
  • EC number
  • Short names
    GO

Gene names

    • Name
      thiO
    • Ordered locus names
      PP_0612

Organism names

Accessions

  • Primary accession
    Q88Q83

Proteomes

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004399581-365Glycine oxidase

Proteomic databases

Interaction

Subunit

Monomer.

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Belongs to the DAO family. ThiO subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    365
  • Mass (Da)
    38,679
  • Last updated
    2003-06-01 v1
  • Checksum
    EC0EC9C3A78B6B56
MSKQVVVVGGGVIGLLTAFNLAAKVGQVVVCDQGEVGRESSWAGGGIVSPLYPWRYSPAVTALAHWSQDFYPQLGERLFASTGVDPEVHTTGLYWLDLDDEAEALAWAAREQRPLSAVDISAAYDAVPVLGPGFKHAIYMAGVANVRNPRLVKSLKAALLALPNVSLREHCQITGFVQEKGRVTGVQTADGVLAADEVVLSAGAWSGDLLRTLGLELPVEPVKGQMILFKCAEDFLPSMVLAKGRYAIPRRDGHILVGSTLEHAGYDKTPTADALESLKASAVELLPELEGATVVAHWAGLRPGSPEGIPYIGPVPGHEGLWLNCGHYRNGLVLAPASCQLFTDLLTGAEPIIDPAPYAPEGRLG

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE015451
EMBL· GenBank· DDBJ
AAN66238.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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