Description:
Endonuclease VIII (DNA glycosylase/AP lyase Nei) (EC 3.2.2.-)(EC 4.2.99.18) (DNA-(apurinic or apyrimidinic site) lyase Nei).
Molecular weight: 29711
View which proteins in this organism that is involved with DNA Repair;
classified after biological processes (using data from the GOA project):
DNA repair( GO:0006281 ) base-excision repair( GO:0006284 )
Important dates:
04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
04-JAN-2005, sequence version 2.
07-MAR-2006, entry version 21.
Phylogenetic order:
Bacteria Proteobacteria Gammaproteobacteria Enterobacteriales Enterobacteriaceae Shigella.
To calculate the pI (Isoelectric point - the pH where a protein has a neutral charge),
go to this page and enter the protein ID (e.g 3MG_ECOLI): http://us.expasy.org/tools/pi_tool.html
Links to references in other databases for protein END8_SHIFL:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | AE005674 | AAN42226.1 | - |
| EMBL | AE016980 | AAP16099.1 | - |
| HSSP | P50465 | 1K3W | |
| SMR | Q83LZ7 | 1-262.1 | |
| GenomeReviews | AE014073_GR | S0596.1 | |
| GenomeReviews | AE005674_GR | SF0583.1 | |
| BioCyc | SFLE198214:AAN42226.1-MONOMER | -.1 | |
| HAMAP | MF_01253 | - | 1. |
| InterPro | IPR000191 | Fapy_DNA_glyco. | |
| InterPro | IPR012319 | Form_DNAglyc_cat. | |
| InterPro | IPR000214 | Fpg_Zn_BS. | |
| Pfam | PF01149 | Fapy_DNA_glyco | 1. |
| Pfam | PF06831 | H2TH | 1. |
| ProDom | PD003680 | Fapy_DNA_glyco | 1. |
| PROSITE | PS51068 | FPG_CAT | 1. |
| PROSITE | PS01242 | ZF_FPG_1 | 1. |
| PROSITE | PS51066 | ZF_FPG_2 | 1. |
Keywords:
Complete proteome; DNA damage; DNA repair; DNA-binding; Glycosidase; Hydrolase; Lyase; Metal-binding; Multifunctional enzyme; Zinc; Zinc-finger.
References:
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX MEDLINE=22272406; PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H.,
RA Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J.,
RA Sun L., Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S.,
RA Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y.,
RA Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2457T / ATCC 700930 / Serotype 2a;
RX MEDLINE=22590274; PubMed=12704152;
RX DOI=10.1128/IAI.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W.,
RA Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A.,
RA Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S.,
RA Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella
RT flexneri serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
Feature:
INIT_MET 0 0 By similarity.
CHAIN 1 262 Endonuclease VIII.
/FTId=PRO_0000170899.
ZN_FING 228 262 FPG-type.
ACT_SITE 1 1 Schiff-base intermediate with DNA (By
similarity).
ACT_SITE 2 2 Proton donor (By similarity).
ACT_SITE 52 52 Proton donor (in beta-elimination) (By
similarity).
ACT_SITE 252 252 Proton donor (in delta-elimination) (By
similarity).
BINDING 69 69 DNA (By similarity).
BINDING 124 124 DNA (By similarity).
BINDING 168 168 DNA (By similarity).
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-dihydrouracyl
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).
-!- CATALYTIC ACTIVITY: Removes damaged bases from DNA, leaving an
abasic site.
-!- 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.
-!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
-!- SIMILARITY: Belongs to the FPG family.
-!- SIMILARITY: Contains 1 FPG-type zinc finger.
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Sequence length: 262
PEGPEIRRAA DNLEAAIKGK PLTDVWFAFP QLKTYQSQLI GQHVTHVETR GKALLTHFPN
GLTLYSHNQL YGVWRVVDTG EEPQTTRVLR VKLQTADKTI LLYSASDIEM LRPEQLTTHP
FLQRVGPDVL DPNLTPEVVK ERLLSPRFRN RQFAGLLLDQ AFLAGLGNYL RVEILWQVGL
TGNHKAKDLN AAQLDALAHA LLEIPRFSYA TRGQVDENKH HGALFRFKVF HRDGELCERC
GGIIEKTTLS SRPFYWCPGC QH