A0A7R8GZA7 · A0A7R8GZA7_LEPSM
- ProteinMultifunctional fusion protein
- GeneNTH1
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids708 (go to sequence)
- Protein existenceInferred from homology
- Annotation score5/5
Function
function
Bifunctional DNA N-glycosylase with associated apurinic/apyrimidinic (AP) lyase function that catalyzes the first step in base excision repair (BER), the primary repair pathway for the repair of oxidative DNA damage. The DNA N-glycosylase activity releases the damaged DNA base from DNA by cleaving the N-glycosidic bond, leaving an AP site. The AP lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination. Primarily recognizes and repairs oxidative base damage of pyrimidines.
Plays an important role in the de novo pathway and in the salvage pathway of purine nucleotide biosynthesis. Catalyzes the first commited step in the biosynthesis of AMP from IMP.
Plays an important role in the de novo pathway of purine nucleotide biosynthesis.
Catalytic activity
- 2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-phospho-2'-deoxyribonucleoside-DNA + H+
Cofactor
Note: Binds 1 Mg2+ ion per subunit.
Pathway
Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2.
Features
Showing features for binding site, active site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 63-69 | GTP (UniProtKB | ChEBI) | ||||
Sequence: GDEGKGK | ||||||
Active site | 64 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 64 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 64-67 | IMP (UniProtKB | ChEBI) | ||||
Sequence: DEGK | ||||||
Binding site | 89-92 | IMP (UniProtKB | ChEBI) | ||||
Sequence: NAGH | ||||||
Binding site | 91 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 91-93 | GTP (UniProtKB | ChEBI) | ||||
Sequence: GHT | ||||||
Active site | 92 | Proton donor | ||||
Sequence: H | ||||||
Binding site | 178 | IMP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 192 | IMP (UniProtKB | ChEBI); ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 267 | IMP (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 282 | IMP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 342-348 | substrate | ||||
Sequence: TTTGRQR | ||||||
Binding site | 346 | IMP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 348 | GTP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 374-376 | GTP (UniProtKB | ChEBI) | ||||
Sequence: KLD | ||||||
Active site | 625 | Nucleophile; for N-glycosylase activity | ||||
Sequence: K | ||||||
Site | 644 | Important for catalytic activity | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrion | |
Cellular Component | nucleus | |
Molecular Function | adenylosuccinate synthase activity | |
Molecular Function | DNA binding | |
Molecular Function | DNA-(apurinic or apyrimidinic site) endonuclease activity | |
Molecular Function | GTP binding | |
Molecular Function | lyase activity | |
Molecular Function | magnesium ion binding | |
Molecular Function | oxidized pyrimidine nucleobase lesion DNA N-glycosylase activity | |
Biological Process | 'de novo' AMP biosynthetic process | |
Biological Process | base-excision repair, AP site formation | |
Biological Process | IMP metabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMultifunctional fusion protein
Including 2 domains:
- Recommended nameAdenylosuccinate synthetase
- EC number
- Short namesAMPSase ; AdSS
- Alternative names
- Recommended nameEndonuclease III homolog
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Crustacea > Multicrustacea > Hexanauplia > Copepoda > Siphonostomatoida > Caligidae > Lepeophtheirus
Accessions
- Primary accessionA0A7R8GZA7
Proteomes
Subcellular Location
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 543-694 | HhH-GPD | ||||
Sequence: LSSQTKDEVNHAAMNRLRGKGLSVEGILSMEDKELEGLIYPVGFYKRKTTYLKKTCEILKKDYDSDIPNTIDDLTKLPGVGPKMAYLVMDIAWNQVVGIGVDTHVHRISNRLKWTGLSGTKNPEDTRKYLEEWLPQSYWKETNWLLVGFGQQ |
Sequence similarities
Belongs to the Nth/MutY family.
Belongs to the adenylosuccinate synthetase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length708
- Mass (Da)79,119
- Last updated2021-06-02 v1
- Checksum669E1F31476132AB
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
HG994580 EMBL· GenBank· DDBJ | CAF2760792.1 EMBL· GenBank· DDBJ | Genomic DNA |