A5ILP7 (OGG1_THEP1) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 35.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Probable N-glycosylase/DNA lyase | ||||
| Gene names |
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| Organism | Thermotoga petrophila (strain RKU-1 / ATCC BAA-488 / DSM 13995) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 390874 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Thermotogae › Thermotogales › Thermotogaceae › Thermotoga › ![]() |
Protein attributes
| Sequence length | 207 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Responsible for removing an oxidatively damaged form of guanine (7,8-dihydro-8-oxoguanine = 7-oxoG) from DNA. Also nicks DNA at apurinic/apyrimidinic sites (AP sites) By similarity. HAMAP-Rule MF_00241 |
| Catalytic activity | The C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate. HAMAP-Rule MF_00241 |
| Sequence similarities | Belongs to the type-2 OGG1 family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | DNA damage DNA repair |
| Molecular function | Glycosidase Hydrolase Lyase |
| Technical term | Complete proteome Multifunctional enzyme |
| Gene Ontology (GO) | |
| Biological_process | base-excision repair Inferred from electronic annotation. Source: HAMAP |
| Molecular_function | DNA-(apurinic or apyrimidinic site) lyase activity Inferred from electronic annotation. Source: HAMAP hydrolase activity, hydrolyzing N-glycosyl compoundsInferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 207 | 207 | Probable N-glycosylase/DNA lyase HAMAP-Rule MF_00241 | PRO_1000005711 | |||||
Sites | |||||||||
| Active site | 129 | 1 | By similarity | ||||||
Sequences
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References
| [1] | "Complete sequence of Thermotoga petrophila RKU-1." US DOE Joint Genome Institute Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Detter J.C., Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L. Richardson P.Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: RKU-1 / ATCC BAA-488 / DSM 13995. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000702 Genomic DNA. Translation: ABQ47120.1. |
| RefSeq | YP_001244696.1. NC_009486.1. |
3D structure databases | |
| ProteinModelPortal | A5ILP7. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 390874.Tpet_1106. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | ABQ47120; ABQ47120; Tpet_1106. |
| GeneID | 5170013. |
| KEGG | tpt:Tpet_1106. |
| PATRIC | 23945024. VBIThePet65348_1122. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG1059. |
| HOGENOM | HOG000224507. |
| KO | K03653. |
| OMA | IIDRHIL. |
| ProtClustDB | PRK01229. |
Family and domain databases | |
| HAMAP | MF_00241. Ogg. |
| InterPro | IPR012092. DNA_glyclase/DNA_lyase_thermo. IPR011257. DNA_glycosylase. IPR003265. HhH-GPD_domain. [Graphical view] |
| Pfam | PF00730. HhH-GPD. 1 hit. [Graphical view] |
| PIRSF | PIRSF005954. Thrmst_ogg. 1 hit. |
| SMART | SM00478. ENDO3c. 1 hit. [Graphical view] |
| SUPFAM | SSF48150. DNA_glycsylse. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | OGG1_THEP1 | ||||||||
| Accession | Primary (citable) accession number: A5ILP7 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
