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Q8X9C6 (END8_ECO57) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended 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:Z0865, ECs0739
OrganismEscherichia coli O157:H7 [Complete proteome] [HAMAP]
Taxonomic identifier83334 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length263 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 263262Endonuclease 8 HAMAP MF_01253
PRO_0000170895

Regions

Zinc finger229 – 26335FPG-type HAMAP MF_01253

Sites

Active site21Schiff-base intermediate with DNA By similarity
Active site31Proton donor By similarity
Active site531Proton donor; for beta-elimination activity By similarity
Active site2531Proton donor; for delta-elimination activity By similarity
Binding site701DNA By similarity
Binding site1251DNA By similarity
Binding site1691DNA By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8X9C6 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 1AC3E46A06E062C9

FASTA26329,811
        10         20         30         40         50         60 
MPEGPEIRRA ADNLEAAIKG KPLTDVWFAF PQLKTYQSQL IGQHVTHVET RGKALLTHFS 

        70         80         90        100        110        120 
NDLTLYSHNQ LYGVWRVVDT GEESQTTRVL RVKLQTADKT ILLYSASDIE MLTPEQLTTH 

       130        140        150        160        170        180 
PFLQRVGPDV LDPNLTPEVV KERLLSPRFR NRQFAGLLLD QAFLAGLGNY LRVEILWQVG 

       190        200        210        220        230        240 
LTGNHKAKDL NAAQLDALAH ALLDIPRFSY ATRGQVDENK HHGALFRFKV FHRDGELCER 

       250        260 
CGGIIEKTTL SSRPFYWCPG CQH

« Hide

References

[1]"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7."
Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. expand/collapse author list , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R.
Nature 409:529-533(2001) [PubMed: 11206551] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
[2]"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. expand/collapse author list , Kuhara S., Shiba T., Hattori M., Shinagawa H.
DNA Res. 8:11-22(2001) [PubMed: 11258796] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE005174 Genomic DNA. Translation: AAG55037.1.
BA000007 Genomic DNA. Translation: BAB34162.1.
PIRA85572.
C90721.
RefSeqNP_286429.1. NC_002655.2.
NP_308766.1. NC_002695.1.

3D structure databases

ProteinModelPortalQ8X9C6.
SMRQ8X9C6. Positions 5-263.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000024930; EBESCP00000023823; EBESCG00000023984.
EBESCT00000056469; EBESCP00000054297; EBESCG00000055517.
GeneID917108.
957808.
GenomeReviewsGene locus Z0865 in contig AE005174_GR.
Gene locus ECs0739 in contig BA000007_GR.
KEGGece:Z0865.
ecs:ECs0739.
PATRIC18350496. VBIEscCol44059_0759.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000011011.
HOGENOMHBG690070.
OMAPRCQPGP.
ProtClustDBPRK10445.

Enzyme and pathway databases

BioCycECOL83334:ECS0739-MONOMER.

Family and domain databases

HAMAPMF_01253. Endonuclease_8.
[Tree]
InterProIPR015886. 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]
KOK05522.
PfamPF01149. Fapy_DNA_glyco. 1 hit.
PF06831. H2TH. 1 hit.
PF06827. zf-FPG_IleRS. 1 hit.
[Graphical view]
SMARTSM00898. Fapy_DNA_glyco. 1 hit.
[Graphical view]
SUPFAMSSF81624. Form_DNAglyc_cat. 1 hit.
SSF46946. Ribosomal_H2TH. 1 hit.
PROSITEPS51068. FPG_CAT. 1 hit.
PS01242. ZF_FPG_1. 1 hit.
PS51066. ZF_FPG_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameEND8_ECO57
AccessionPrimary (citable) accession number: Q8X9C6
Entry history
Integrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: January 23, 2007
Last modified: January 25, 2012
This is version 75 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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