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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: 29680
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:
06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
06-JUN-2002, sequence version 2.
07-MAR-2006, entry version 31.
Phylogenetic order:
Bacteria Proteobacteria Gammaproteobacteria Enterobacteriales Enterobacteriaceae Escherichia.
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_ECO57:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | AE005174 | AAG55037.1 | - |
| EMBL | BA000007 | BAB34162.1 | - |
| PIR | A85572 | A85572. | |
| PIR | C90721 | C90721. | |
| HSSP | P50465 | 1K3W | |
| SMR | Q8X9C6 | 1-262.1 | |
| GenomeReviews | BA000007_GR | ECs0739.1 | |
| GenomeReviews | AE005174_GR | z0865.1 | |
| BioCyc | ECOL83334-1:ECS0739-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=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX MEDLINE=21074935; PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA Welch R.A., Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX MEDLINE=21156231; PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli
RT O157:H7 and genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
Feature:
INIT_MET 0 0 By similarity.
CHAIN 1 262 Endonuclease VIII.
/FTId=PRO_0000170895.
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 GKALLTHFSN
DLTLYSHNQL YGVWRVVDTG EESQTTRVLR VKLQTADKTI LLYSASDIEM LTPEQLTTHP
FLQRVGPDVL DPNLTPEVVK ERLLSPRFRN RQFAGLLLDQ AFLAGLGNYL RVEILWQVGL
TGNHKAKDLN AAQLDALAHA LLDIPRFSYA TRGQVDENKH HGALFRFKVF HRDGELCERC
GGIIEKTTLS SRPFYWCPGC QH