O58954

PR
Gene name
PH1229
Protein name
N-glycosylase/DNA lyase
Names
8-oxoguanine DNA glycosylase, AGOG, DNA-(apurinic or apyrimidinic site) lyase, AP lyase
Species
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
KEGG Pathway
pho:PH1229
EC number
4.2.99.18: Other carbon-oxygen lyases
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

167-239 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for O58954

Entry ID Method Resolution Chain Position Source
AF-O58954-F1 Predicted AlphaFoldDB

No variants for O58954

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for O58954

No associated diseases with O58954

No regional properties for O58954

Type Name Position InterPro Accession
No domain, repeats, and functional sites for O58954

Functions

Description
EC Number 4.2.99.18 Other carbon-oxygen lyases
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

2 GO annotations of molecular function

Name Definition
class I DNA-(apurinic or apyrimidinic site) endonuclease activity Catalysis of the cleavage of an AP site 3' of the baseless site by a beta-lyase mechanism, leaving an unsaturated aldehyde, termed a 3'-(4-hydroxy-5-phospho-2-pentenal) residue, and a 5'-phosphate.
oxidized base lesion DNA N-glycosylase activity Catalysis of the removal of oxidized bases by cleaving the N-C1' glycosidic bond between the target damaged DNA base and the deoxyribose sugar. The reaction releases a free base and leaves an apurinic/apyrimidinic (AP) site.

1 GO annotations of biological process

Name Definition
base-excision repair In base excision repair, an altered base is removed by a DNA glycosylase enzyme, followed by excision of the resulting sugar phosphate. The small gap left in the DNA helix is filled in by the sequential action of DNA polymerase and DNA ligase.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MIAELIREIG IEGARFIEEN IDEQFKALSY LSEGMDRVNF VRLVIANALV SYQLTGKGEM
70 80 90 100 110 120
WWWEFAKYFK GKEVKTIYSA YKEFLPNSKF NRRLIQQKLL RIKKIEPFLS TLTEESIERY
130 140 150 160 170 180
YEDMTLLWKA IAKVLKVDRE SKTVVFSVKM FGYAARIVLS KFNPYPMEIP IPEDVRIIKL
190 200 210 220 230
TRKLTNERPR DFWMKIAKES NVPPLHIDSI LWPLLGGARV EEAPPELKEK LEKLIRVIR