Q8FJU5 (END8_ECOL6) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Endonuclease 8

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

Gene names

Name:	nei
Ordered Locus Names:	c0793

Organism

Escherichia coli O6 [Complete proteome] [HAMAP]

Taxonomic identifier

217992 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	263 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 a preference for oxidized pyrimidines, such as thymine glycol, 5,6-dihydrouracil and 5,6-dihydrothymine. 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. HAMAP MF_01253
Catalytic activity	Removes damaged bases from DNA, leaving an abasic site. HAMAP MF_01253 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 MF_01253
Cofactor	Binds 1 zinc ion per subunit By similarity. HAMAP MF_01253
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 endonuclease activity 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 – 263	262	Endonuclease 8 HAMAP MF_01253		PRO_0000170894
Regions
	Zinc finger	229 – 263	35	FPG-type HAMAP MF_01253
Sites
	Active site	2	1	Schiff-base intermediate with DNA By similarity
	Active site	3	1	Proton donor By similarity
	Active site	53	1	Proton donor; for beta-elimination activity By similarity
	Active site	253	1	Proton donor; for delta-elimination activity By similarity
	Binding site	70	1	DNA By similarity
	Binding site	125	1	DNA By similarity
	Binding site	169	1	DNA By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8FJU5 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 0D8EFFCBC8DD1A27	FASTA	263	29,811
	10 20 30 40 50 60 MPEGPEIRRA ADNLEAAIKG KPLTDVWFAF PQLKSYQSRL IGQHVTHVET RGKALLTHFS 70 80 90 100 110 120 NDLTLYSHNQ LYGVWRVVDT GEEPQTTRVL RVKLQTADKT ILLYSASDIE MLTPEQLTTH 130 140 150 160 170 180 PFLQRVGPDV LDPNLTPEVV KERLLSPRFR NRQFAGLLLD QAFLAGLGNY LRVEILWQVG 190 200 210 220 230 240 LTGNHKAKDL NAAQLDALAH ALLDIPRLSY ATRGQVDENK YHGALFRFKV FHRDGEPCER 250 260 CGGIIEKTTL SSRPFYWCPG CQH

References

[1]

"Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli." Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R. Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002) [PubMed: 12471157] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O6:H1 / CFT073 / ATCC 700928 / UPEC.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE014075 Genomic DNA. Translation: AAN79266.1.
RefSeq	NP_752723.1. NC_004431.1.
3D structure databases
ProteinModelPortal	Q8FJU5.
SMR	Q8FJU5. Positions 2-263.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000043496; EBESCP00000041845; EBESCG00000042546.
GeneID	1035763.
GenomeReviews	Gene locus c0793 in contig AE014075_GR.
KEGG	ecc:c0793.
PATRIC	18279641. VBIEscCol75197_0757.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000011011.
HOGENOM	HBG690070.
OMA	PRCQPGP.
ProtClustDB	PRK10445.
Family and domain databases
HAMAP	MF_01253. Endonuclease_8. [Tree]
InterPro	IPR015886. DNA_glyclase/AP_lyase_DNA-bd. IPR015887. DNA_glyclase_Znf_dom_DNA_BS. IPR012319. DNA_glycosylase/AP_lyase_cat. IPR023713. Endonuclease-VIII. IPR010979. Ribosomal_S13-like_H2TH. IPR000214. Znf_DNA_glyclase/AP_lyase. IPR010663. Znf_DNA_glyclase/IsotRNA_synth. [Graphical view]
KO	K05522.
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. 1 hit. PS01242. ZF_FPG_1. 1 hit. PS51066. ZF_FPG_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

END8_ECOL6

Accession

Primary (citable) accession number: Q8FJU5

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 4, 2005
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 66 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program