A0A9D3XAF9 · A0A9D3XAF9_9SAUR

Function

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

  • H2O + N2-(1-hydroxy-2-oxoethyl)-GDP = GDP + glycolate + H+
  • H2O + N2-(1-hydroxy-2-oxoethyl)-GMP = glycolate + GMP + H+
  • H2O + N2-(1-hydroxy-2-oxoethyl)-GTP = glycolate + GTP + H+
  • H2O + N2-(1-hydroxy-2-oxoethyl)-dGTP = dGTP + glycolate + H+
  • H2O + N2-(1-hydroxy-2-oxopropyl)-GDP = GDP + H+ + lactate
  • H2O + N2-(1-hydroxy-2-oxopropyl)-GMP = GMP + H+ + lactate
  • H2O + N2-(1-hydroxy-2-oxopropyl)-GTP = GTP + H+ + lactate
  • H2O + N2-(1-hydroxy-2-oxopropyl)-dGTP = dGTP + H+ + lactate
  • H2O + N6-(1-hydroxy-2-oxoethyl)-L-lysyl-[protein] = glycolate + H+ + L-lysyl-[protein]
    EC:3.5.1.124 (UniProtKB | ENZYME | Rhea)
  • H2O + N6-(1-hydroxy-2-oxopropyl)-L-lysyl-[protein] = H+ + L-lysyl-[protein] + lactate
    EC:3.5.1.124 (UniProtKB | ENZYME | Rhea)
  • H2O + N(omega)-(1-hydroxy-2-oxoethyl)-L-arginyl-[protein] = glycolate + H+ + L-arginyl-[protein]
    EC:3.5.1.124 (UniProtKB | ENZYME | Rhea)
  • H2O + N(omega)-(1-hydroxy-2-oxopropyl)-L-arginyl-[protein] = H+ + L-arginyl-[protein] + lactate
    EC:3.5.1.124 (UniProtKB | ENZYME | Rhea)
  • H2O + S-(1-hydroxy-2-oxoethyl)-L-cysteinyl-[protein] = glycolate + H+ + L-cysteinyl-[protein]
    EC:3.5.1.124 (UniProtKB | ENZYME | Rhea)
  • H2O + S-(1-hydroxy-2-oxopropyl)-L-cysteinyl-[protein] = H+ + L-cysteinyl-[protein] + lactate
    EC:3.5.1.124 (UniProtKB | ENZYME | Rhea)
  • an N2-(1-hydroxy-2-oxoethyl)-2'-deoxyguanosine in DNA + H2O = a 2'-deoxyguanosine in DNA + glycolate + H+
  • an N2-(1-hydroxy-2-oxoethyl)-guanosine in RNA + H2O = a guanosine in RNA + glycolate + H+
  • an N2-(1-hydroxy-2-oxopropyl)-2'-deoxyguanosine in DNA + H2O = a 2'-deoxyguanosine in DNA + H+ + lactate
  • an N2-(1-hydroxy-2-oxopropyl)-guanosine in RNA + H2O = a guanosine in RNA + H+ + lactate

GO annotations

AspectTerm
Cellular Componentmembrane raft
Cellular Componentmitochondrion
Cellular Componentnucleus
Molecular Functionoxidoreductase activity, acting on peroxide as acceptor
Biological Processautophagy
Biological Processglycolate biosynthetic process
Biological Processglyoxal metabolic process
Biological Processinflammatory response
Biological Processresponse to oxidative stress
Biological Processsingle fertilization

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    protein deglycase
  • EC number
  • Alternative names
    • Maillard deglycase
    • Parkinsonism-associated deglycase

Gene names

    • ORF names
      KIL84_022170

Organism names

  • Taxonomic identifier
  • Strain
    • MM-2020
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Archelosauria > Testudinata > Testudines > Cryptodira > Durocryptodira > Testudinoidea > Geoemydidae > Geoemydinae > Mauremys

Accessions

  • Primary accession
    A0A9D3XAF9

Proteomes

Subcellular Location

Membrane raft
Membrane
; Lipid-anchor

PTM/Processing

Keywords

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain4-170DJ-1/PfpI

Sequence similarities

Belongs to the peptidase C56 family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    189
  • Mass (Da)
    20,221
  • Last updated
    2023-05-03 v1
  • Checksum
    1BEF5791063B4DFC
MASKRALVILAKGAEEMETVIPTDVMRRAGIKVTIAGLTGKDPVQCSRDVFICPDASLEDARKEGPYDVVVLPGGNLGAQNLSESPAVKDILVDQENRKGLIAAICAGPTALMAHGIGFGRKVTTHPLAKDKMMKGEHYKYSESRVEKDGNFLTSRGPGTSFEFGLAIVEILMGKEVADQVKAPLILKD

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JAHDVG010000476
EMBL· GenBank· DDBJ
KAH1175645.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp