P64156 (END8B_MYCTU) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 64.
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: Endonuclease 8 2 | ||||||||
| Gene names |
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| Organism | Mycobacterium tuberculosis [Reference proteome] [HAMAP] | ||||||||
| Taxonomic identifier | 1773 [NCBI] | ||||||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex![]() |
Protein attributes
| Sequence length | 255 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. 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 By similarity. Complements an E.coli nei nth double mutant (Ref.4). Ref.3 Ref.4 |
| Catalytic activity | Removes damaged bases from DNA, leaving an abasic site. 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. |
| Cofactor | Binds 1 zinc ion per subunit By similarity. |
| Sequence similarities | Belongs to the FPG family. Contains 1 FPG-type zinc finger. |
| Caution | There are 2 paralogs in M.tuberculosis, in a reference this gene is called nei1 (Ref.3). |
Ontologies
| Keywords | |
|---|---|
| Biological process | DNA damage DNA repair |
| Domain | Zinc-finger |
| Ligand | DNA-binding Metal-binding Zinc |
| Molecular function | Glycosidase Hydrolase Lyase |
| Technical term | Complete proteome Multifunctional enzyme Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | DNA repair Inferred from direct assay Ref.4. Source: MTBBASE base-excision repairInferred from electronic annotation. Source: InterPro nucleotide-excision repairInferred from electronic annotation. Source: InterPro |
| Molecular_function | DNA N-glycosylase activity Inferred from direct assay Ref.4. Source: MTBBASE DNA-(apurinic or apyrimidinic site) lyase activityInferred from electronic annotation. Source: EC damaged DNA bindingInferred from electronic annotation. Source: InterPro double-stranded DNA bindingInferred from direct assay Ref.4. Source: MTBBASE zinc ion bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed By similarity | ||||||
| Chain | 2 – 255 | 254 | Endonuclease 8 2 | PRO_0000170901 | |||||
Regions | |||||||||
| Zinc finger | 221 – 255 | 35 | FPG-type | ||||||
Sites | |||||||||
| Active site | 2 | 1 | Schiff-base intermediate with DNA By similarity | ||||||
| Active site | 3 | 1 | Proton donor By similarity | ||||||
| Active site | 51 | 1 | Proton donor; for beta-elimination activity By similarity | ||||||
| Active site | 245 | 1 | Proton donor; for delta-elimination activity By similarity | ||||||
| Binding site | 67 | 1 | DNA By similarity | ||||||
| Binding site | 164 | 1 | DNA By similarity | ||||||
Sequences
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References
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BX842582 Genomic DNA. Translation: CAB07061.1. AE000516 Genomic DNA. Translation: AAK47739.1. AL123456 Genomic DNA. Translation: CCP46116.1. |
| PIR | B70982. |
| RefSeq | NP_217814.1. NC_000962.3. NP_337925.1. NC_002755.2. YP_006516774.1. NC_018143.1. |
3D structure databases | |
| ProteinModelPortal | P64156. |
| SMR | P64156. Positions 2-254. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 83332.Rv3297. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBMYCT00000002647; EBMYCP00000002647; EBMYCG00000002645. EBMYCT00000071901; EBMYCP00000069960; EBMYCG00000071896. |
| GeneID | 13318120. 887937. 926657. |
| KEGG | mtc:MT3396. mtu:Rv3297. mtv:RVBD_3297. |
| PATRIC | 18129220. VBIMycTub22151_3706. |
Organism-specific databases | |
| TubercuList | Rv3297. |
Phylogenomic databases | |
| eggNOG | COG0266. |
| HOGENOM | HOG000020880. |
| KO | K05522. |
| OMA | WFAFPEL. |
| ProtClustDB | CLSK792413. |
Family and domain databases | |
| InterPro | IPR015886. DNA_glyclase/AP_lyase_DNA-bd. IPR015887. DNA_glyclase_Znf_dom_DNA_BS. IPR012319. DNA_glycosylase/AP_lyase_cat. IPR010979. Ribosomal_S13-like_H2TH. IPR000214. Znf_DNA_glyclase/AP_lyase. [Graphical view] |
| Pfam | PF01149. Fapy_DNA_glyco. 1 hit. PF06831. H2TH. 1 hit. [Graphical view] |
| SMART | SM00898. Fapy_DNA_glyco. 1 hit. [Graphical view] |
| SUPFAM | SSF81624. Form_DNAglyc_cat. 1 hit. SSF46946. Ribosomal_H2TH. 1 hit. |
| PROSITE | PS51068. FPG_CAT. 1 hit. PS01242. ZF_FPG_1. 1 hit. PS51066. ZF_FPG_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | END8B_MYCTU | ||||||||
| Accession | Primary (citable) accession number: P64156 Secondary accession number(s): L0TDQ8, P96902 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names |
| SIMILARITY comments Index of protein domains and families |

Clusters with
