Protein data for FPG_SHIFL:

Description:
Formamidopyrimidine-DNA glycosylase (EC 3.2.2.23) (Fapy-DNAglycosylase) (DNA-(apurinic or apyrimidinic site) lyase mutM)(EC 4.2.99.18) (AP lyase mutM).

Molecular weight: 30129

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:
11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
21-DEC-2004, sequence version 2.
07-MAR-2006, entry version 14.

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 FPG_SHIFL:

DatabasePointerAdd. info#1Add. info#2
EMBLAE005674AAN45121.1ALT_INIT
EMBLAE016991AAP19071.1-
HSSPP055231K82
SMRP641491-268.1
GenomeReviewsAE014073_GRS4094.1
GenomeReviewsAE005674_GRSF3674.1
HAMAPMF_00103-1.
InterProIPR000191Fapy_DNA_glyco.
InterProIPR012319Form_DNAglyc_cat.
InterProIPR000214Fpg_Zn_BS.
InterProIPR010663Znf_Fpg.
PfamPF01149Fapy_DNA_glyco1.
PfamPF06831H2TH1.
PfamPF06827zf-FPG_IleRS1.
ProDomPD003680Fapy_DNA_glyco1.
TIGRFAMsTIGR00577fpg1.
PROSITEPS51068FPG_CAT1.
PROSITEPS01242ZF_FPG_11.
PROSITEPS51066ZF_FPG_21.

General information about the databases mentioned above

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 1 268 Formamidopyrimidine-DNA glycosylase.
/FTId=PRO_0000170863.
ZN_FING 234 268 FPG-type.
ACT_SITE 1 1 Schiff-base intermediate with DNA (By
similarity).
ACT_SITE 2 2 Proton donor (By similarity).
ACT_SITE 56 56 Proton donor (in beta-elimination) (By
similarity).
ACT_SITE 258 258 Proton donor (in delta-elimination) (By
similarity).
BINDING 89 89 DNA (By similarity).
BINDING 108 108 DNA (By similarity).
BINDING 149 149 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 purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). 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: Hydrolysis of DNA containing ring-opened N(7)-
methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-
methyl)formamidopyrimidine.
-!- 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).
-!- SUBUNIT: Monomer (By similarity).
-!- SIMILARITY: Belongs to the FPG family.
-!- SIMILARITY: Contains 1 FPG-type zinc finger.
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Sequence length: 268

     PELPEVETSR RGIEPHLVGA TILHAVVRNG RLRWPVSEEI YRLSDQPVLS VQRRAKYLLL
     ELPEGWIIIH LGMSGSLRIL PEELPPEKHD HVDLVMSNGK VLRYTDPRRF GAWLWTKELE
     GHNVLAHLGP EPLSDDFNGE YLHQKCAKKK TAIKPWLMDN KLVVGVGNIY ASESLFAAGI
     HPDRLASSLS LAECELLARV IKAVLLRSIE QGGTTLKDFL QSDGKPGYFA QELQVYGRKG
     EPCRVCGTPI VATKHAQRAT FYCRQCQK