O80358 · FPG_ARATH
- ProteinFormamidopyrimidine-DNA glycosylase
- GeneFPG1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids390 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as a DNA glycosylase that recognizes and removes damaged bases. Can process efficiently 4,6-diamino-5-formamidopyrimidine (FapyA), 2,6-diamino-4- hydroxy-5-formamidopyrimidine (FapyG) and the further oxidation products of 8-oxoguanine (8-oxoG), such as guanidinohydantoin and spiroiminodihydantoin. Has marginal activity towards 8-oxoG. Has AP (apurinic/apyrimidinic) lyase activity. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates.
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+
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 2 | Schiff-base intermediate with DNA | ||||
Sequence: P | ||||||
Active site | 3 | Proton donor | ||||
Sequence: E | ||||||
Active site | 60 | Proton donor; for beta-elimination activity | ||||
Sequence: K | ||||||
Binding site | 107 | DNA (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 126 | DNA (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 167 | DNA (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 186 | DNA (UniProtKB | ChEBI) | ||||
Sequence: N |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | nucleus | |
Molecular Function | class I DNA-(apurinic or apyrimidinic site) endonuclease activity | |
Molecular Function | damaged DNA binding | |
Molecular Function | DNA N-glycosylase activity | |
Molecular Function | oxidized purine nucleobase lesion DNA N-glycosylase activity | |
Molecular Function | zinc ion binding | |
Biological Process | base-excision repair | |
Biological Process | DNA repair | |
Biological Process | response to oxidative stress |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameFormamidopyrimidine-DNA glycosylase
- EC number
- Short namesFapy-DNA glycosylase
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionO80358
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
Phenotypes & Variants
Disruption phenotype
No visible phenotype under normal growth conditions or UV-A irradiation stress.
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 38 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for initiator methionine, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Chain | PRO_0000421261 | 2-390 | Formamidopyrimidine-DNA glycosylase | |||
Sequence: PELPEVEAARRAIEENCLGKKIKRVIIADDNKVIHGISPSDFQTSILGKTIISARRKGKNLWLELDSPPFPSFQFGMAGAIYIKGVAVTKYKRSAVKDSEEWPSKYSKFFVELDDGLELSFTDKRRFAKVRLLANPTSVSPISELGPDALLEPMTVDEFAESLAKKKITIKPLLLDQGYISGIGNWIADEVLYQARIHPLQTASSLSKEQCEALHTSIKEVIEKAVEVDADSSQFPSYWIFHNREKKPGKAFVDGKKIDFITAGGRTTAYVPELQKLYGKDAEKAAKVRPAKRGVKPKEDDGDGEEDEQETEKEDESAKSKKGQKPRGGRGKKPASKTKTEESDDDGDDSEAEEEVVKPKGRGTKPAIKRKSEEKATSQAGKKPKGRKS |
Proteomic databases
PTM databases
Expression
Interaction
Structure
Family & Domains
Features
Showing features for compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 283-301 | Basic and acidic residues | ||||
Sequence: AEKAAKVRPAKRGVKPKED | ||||||
Region | 283-390 | Disordered | ||||
Sequence: AEKAAKVRPAKRGVKPKEDDGDGEEDEQETEKEDESAKSKKGQKPRGGRGKKPASKTKTEESDDDGDDSEAEEEVVKPKGRGTKPAIKRKSEEKATSQAGKKPKGRKS | ||||||
Compositional bias | 354-382 | Basic and acidic residues | ||||
Sequence: EEEVVKPKGRGTKPAIKRKSEEKATSQAG |
Sequence similarities
Belongs to the FPG family.
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
O80358-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length390
- Mass (Da)43,194
- Last updated1998-11-01 v1
- ChecksumF6B5E0DAFD6FD010
O80358-2
- Name2
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A1P8AVR7 | A0A1P8AVR7_ARATH | MMH-1 | 288 | ||
A0A178VZV9 | A0A178VZV9_ARATH | MMH-1 | 224 |
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_045377 | 224-274 | in isoform 2 | |||
Sequence: EKAVEVDADSSQFPSYWIFHNREKKPGKAFVDGKKIDFITAGGRTTAYVPE → QHAVQVNADSKEFPVEWLFHFRWGKKAGKVNGKLSHHLSINLMKQNLGFCR | ||||||
Sequence conflict | 239 | in Ref. 2; AAC97952 | ||||
Sequence: Y → N | ||||||
Alternative sequence | VSP_045378 | 275-390 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 283-301 | Basic and acidic residues | ||||
Sequence: AEKAAKVRPAKRGVKPKED | ||||||
Compositional bias | 354-382 | Basic and acidic residues | ||||
Sequence: EEEVVKPKGRGTKPAIKRKSEEKATSQAG |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB010690 EMBL· GenBank· DDBJ | BAA32702.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AB010690 EMBL· GenBank· DDBJ | BAA32703.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF099970 EMBL· GenBank· DDBJ | AAC97952.1 EMBL· GenBank· DDBJ | mRNA | ||
AF099971 EMBL· GenBank· DDBJ | AAC97953.1 EMBL· GenBank· DDBJ | mRNA | ||
AC008016 EMBL· GenBank· DDBJ | AAD55612.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AC008016 EMBL· GenBank· DDBJ | AAD55613.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002684 EMBL· GenBank· DDBJ | AEE32814.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002684 EMBL· GenBank· DDBJ | AEE32815.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002684 EMBL· GenBank· DDBJ | ANM60729.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BT043496 EMBL· GenBank· DDBJ | ACG58696.1 EMBL· GenBank· DDBJ | mRNA |