A0A9D3XAF9 · A0A9D3XAF9_9SAUR
- Proteinprotein deglycase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids189 (go to sequence)
- Protein existenceInferred from homology
- Annotation score5/5
Function
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
- 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
Aspect | Term | |
---|---|---|
Cellular Component | membrane raft | |
Cellular Component | mitochondrion | |
Cellular Component | nucleus | |
Molecular Function | oxidoreductase activity, acting on peroxide as acceptor | |
Biological Process | autophagy | |
Biological Process | glycolate biosynthetic process | |
Biological Process | glyoxal metabolic process | |
Biological Process | inflammatory response | |
Biological Process | response to oxidative stress | |
Biological Process | single fertilization |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameprotein deglycase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Archelosauria > Testudinata > Testudines > Cryptodira > Durocryptodira > Testudinoidea > Geoemydidae > Geoemydinae > Mauremys
Accessions
- Primary accessionA0A9D3XAF9
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Lipid-anchor
PTM/Processing
Keywords
- PTM
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 4-170 | DJ-1/PfpI | ||||
Sequence: KRALVILAKGAEEMETVIPTDVMRRAGIKVTIAGLTGKDPVQCSRDVFICPDASLEDARKEGPYDVVVLPGGNLGAQNLSESPAVKDILVDQENRKGLIAAICAGPTALMAHGIGFGRKVTTHPLAKDKMMKGEHYKYSESRVEKDGNFLTSRGPGTSFEFGLAIVE |
Sequence similarities
Belongs to the peptidase C56 family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length189
- Mass (Da)20,221
- Last updated2023-05-03 v1
- Checksum1BEF5791063B4DFC
Keywords
- Technical term