P64159 (END8A_MYCBO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Endonuclease 8 1

Alternative name(s):
DNA glycosylase/AP lyase Nei 1
EC=3.2.2.-
DNA-(apurinic or apyrimidinic site) lyase Nei 1
EC=4.2.99.18
Endonuclease VIII 1

Gene names

Name:	nei1
Ordered Locus Names:	Mb2491c

Organism

Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97) [Complete proteome] [HAMAP]

Taxonomic identifier

233413 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex › Mycobacterium bovis

Protein attributes

Sequence length	268 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.
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.

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
Gene Ontology (GO)
Biological_process	base-excision repair Inferred from electronic annotation. Source: InterPro nucleotide-excision repair Inferred from electronic annotation. Source: InterPro
Molecular_function	DNA-(apurinic or apyrimidinic site) lyase activity Inferred from electronic annotation. Source: EC damaged DNA binding Inferred from electronic annotation. Source: InterPro hydrolase activity, hydrolyzing N-glycosyl compounds Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred 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 – 268	267	Endonuclease 8 1		PRO_0000170904
Regions
	Zinc finger	234 – 268	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	52	1	Proton donor; for beta-elimination activity By similarity
	Active site	258	1	Proton donor; for delta-elimination activity By similarity
	Binding site	125	1	DNA By similarity
	Binding site	166	1	DNA By similarity

Sequences

	Sequence		Length	Mass (Da)
	P64159 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 1142DE185BD14F24	FASTA	268	29,714
	10 20 30 40 50 60 MPEGHTLHRL ARLHQRRFAG APVSVSSPQG RFADSASALN GRVLRRASAW GKHLFHHYVG 70 80 90 100 110 120 GPVVHVHLGL YGTFTEWARP TDGWLPEPAG QVRMRMVGAE FGTDLRGPTV CESIDDGEVA 130 140 150 160 170 180 DVVARLGPDP LRSDANPSSA WSRITKSRRP IGALLMDQTV IAGVGNVYRN ELLFRHRIDP 190 200 210 220 230 240 QRPGRGIGEP EFDAAWNDLV SLMKVGLRRG KIIVVRPEHD HGLPSYLPDR PRTYVYRRAG 250 260 EPCRVCGGVI RTALLEGRNV FWCPVCQT

References

[1]

"The complete genome sequence of Mycobacterium bovis." Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M., Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B., Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J. , Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G. Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-935 / AF2122/97.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX248342 Genomic DNA. Translation: CAD97352.1.
RefSeq	NP_856138.1. NC_002945.3.
3D structure databases
ProteinModelPortal	P64159.
SMR	P64159. Positions 2-267.
ModBase	Search...
Protein-protein interaction databases
STRING	233413.Mb2491c.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBMYCT00000017286; EBMYCP00000017121; EBMYCG00000017281.
GeneID	1094219.
KEGG	mbo:Mb2491c.
PATRIC	18007203. VBIMycBov88188_2742.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0266.
HOGENOM	HOG000020880.
KO	K05522.
OMA	HTPEAMG.
ProtClustDB	CLSK791864.
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. IPR010663. Znf_DNA_glyclase/IsotRNA_synth. [Graphical view]
Pfam	PF01149. Fapy_DNA_glyco. 1 hit. PF06831. H2TH. 1 hit. PF06827. zf-FPG_IleRS. 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. False negative. PS01242. ZF_FPG_1. 1 hit. PS51066. ZF_FPG_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

END8A_MYCBO

Accession

Primary (citable) accession number: P64159
Secondary accession number(s): O53191

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 65 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program