Q9X2E1 (OGG1_THEMA) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 75.
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 |
| ||||
| Organism | Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099) [Reference proteome] [HAMAP] | ||||
| Taxonomic identifier | 243274 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Thermotogae › Thermotogales › Thermotogaceae › Thermotoga › ![]() |
Protein attributes
| Sequence length | 207 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
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 | 3D-structure Complete proteome Multifunctional enzyme Reference proteome |
| 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_0000159572 | |||||||||||||||||||||||||||||||
Sites | |||||||||||||||||||||||||||||||||||
| Active site | 129 | 1 | By similarity | ||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||
| Helix | 1 – 32 | 32 | |||||||||||||||||||||||||||||||||
| Helix | 35 – 47 | 13 | |||||||||||||||||||||||||||||||||
| Turn | 48 – 50 | 3 | |||||||||||||||||||||||||||||||||
| Helix | 53 – 63 | 11 | |||||||||||||||||||||||||||||||||
| Helix | 66 – 69 | 4 | |||||||||||||||||||||||||||||||||
| Helix | 72 – 81 | 10 | |||||||||||||||||||||||||||||||||
| Helix | 87 – 97 | 11 | |||||||||||||||||||||||||||||||||
| Helix | 98 – 100 | 3 | |||||||||||||||||||||||||||||||||
| Turn | 101 – 103 | 3 | |||||||||||||||||||||||||||||||||
| Helix | 104 – 109 | 6 | |||||||||||||||||||||||||||||||||
| Helix | 112 – 122 | 11 | |||||||||||||||||||||||||||||||||
| Helix | 128 – 136 | 9 | |||||||||||||||||||||||||||||||||
| Turn | 137 – 139 | 3 | |||||||||||||||||||||||||||||||||
| Helix | 148 – 156 | 9 | |||||||||||||||||||||||||||||||||
| Helix | 169 – 186 | 18 | |||||||||||||||||||||||||||||||||
| Helix | 190 – 202 | 13 | |||||||||||||||||||||||||||||||||
Sequences
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References
| [1] | "Evidence for lateral gene transfer between Archaea and Bacteria from genome sequence of Thermotoga maritima." Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., Cotton M.D., Pratt M.S. Fraser C.M.Nature 399:323-329(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | AE000512 Genomic DNA. Translation: AAD36884.1. | ||||||||||||
| PIR | H72206. | ||||||||||||
| RefSeq | NP_229618.1. NC_000853.1. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | Q9X2E1. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| STRING | 243274.TM1821. | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| EnsemblBacteria | AAD36884; AAD36884; TM_1821. | ||||||||||||
| GeneID | 897824. | ||||||||||||
| KEGG | tma:TM1821. | ||||||||||||
| PATRIC | 23938629. VBITheMar51294_1841. | ||||||||||||
Phylogenomic databases | |||||||||||||
| eggNOG | COG1059. | ||||||||||||
| 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... | ||||||||||||
Other | |||||||||||||
| EvolutionaryTrace | Q9X2E1. | ||||||||||||
Entry information
| Entry name | OGG1_THEMA | ||||||||
| Accession | Primary (citable) accession number: Q9X2E1 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
