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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: 29734
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 35.
Phylogenetic order:
Bacteria Proteobacteria Gammaproteobacteria Enterobacteriales Enterobacteriaceae Salmonella.
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_SALTI:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | AL627268 | CAD05190.1 | - |
| EMBL | AE014613 | AAO69762.1 | - |
| HSSP | P50465 | 1K3X | |
| SMR | Q8Z8D2 | 1-261.1 | |
| GenomeReviews | AL513382_GR | STY0771.1 | |
| GenomeReviews | AE014613_GR | t2148.1 | |
| BioCyc | SENT209261:T2148-MONOMER | -.1 | |
| BioCyc | SENT90370:STY0771-MONOMER | -.1 | |
| HAMAP | MF_01253 | - | 1. |
| InterPro | IPR000191 | Fapy_DNA_glyco. | |
| InterPro | IPR012319 | Form_DNAglyc_cat. | |
| InterPro | IPR000214 | Fpg_Zn_BS. | |
| InterPro | IPR010663 | Znf_Fpg. | |
| Pfam | PF01149 | Fapy_DNA_glyco | 1. |
| Pfam | PF06831 | H2TH | 1. |
| Pfam | PF06827 | zf-FPG_IleRS | 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=CT18;
RX MEDLINE=21534947; PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P.,
RA Cronin A., Davis P., Davies R.M., Dowd L., White N., Farrar J.,
RA Feltwell T., Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K.,
RA Krogh A., Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C.,
RA Quail M.A., Rutherford K.M., Simmonds M., Skelton J., Stevens K.,
RA Whitehead S., Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella
RT enterica serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ty2 / ATCC 700931;
RX MEDLINE=22531367; PubMed=12644504;
RX DOI=10.1128/JB.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J.,
RA Burland V., Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2
RT and CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
Feature:
INIT_MET 0 0 By similarity.
CHAIN 1 262 Endonuclease VIII.
/FTId=PRO_0000170897.
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 PLTDVWFAFA QLKPYESQLT GQLVTRIETR GKALLTHFSN
GLTLYSHNQL YGVWRVIDTG EIPQTTRILR VRLQTADKII LLYSASDIEM LTAEQLMTHP
FLQRVGPDVL DARLTPEEVK ARLLSPRFRN RQFSGLLLDQ SFLAGLGNYL RVEILWQVGL
TGQHKAKDLN EAQLNALSHA LLDIPRLSYT TRGQADENKH HGALFRFKVF HRDGEACERC
GGIIEKTTLS SRPFYWCAHC QK