Protein data for FPG_LACPL:

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: 30761

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:
31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
21-DEC-2004, sequence version 2.
07-MAR-2006, entry version 22.

Phylogenetic order:
Bacteria Firmicutes Lactobacillales Lactobacillaceae Lactobacillus.

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_LACPL:

DatabasePointerAdd. info#1Add. info#2
EMBLAL935256CAD63963.1-
HSSPP423711KFV
GenomeReviewsAL935263_GRlp_1509.1
BioCycLPLA220668:LP_1509-MONOMER-.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_1FALSE_NEG.
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=NCIMB 8826 / WCFS1;
RX MEDLINE=22480296; PubMed=12566566; DOI=10.1073/pnas.0337704100;
RA Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D.,
RA Kuipers O.P., Leer R., Tarchini R., Peters S.A., Sandbrink H.M.,
RA Fiers M.W.E.J., Stiekema W., Klein Lankhorst R.M., Bron P.A.,
RA Hoffer S.M., Nierop Groot M.N., Kerkhoven R., De Vries M., Ursing B.,
RA De Vos W.M., Siezen R.J.;
RT "Complete genome sequence of Lactobacillus plantarum WCFS1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003).

Feature:
INIT_MET 0 0 By similarity.
CHAIN 1 273 Formamidopyrimidine-DNA glycosylase.
/FTId=PRO_0000170831.
ZN_FING 238 272 FPG-type.
ACT_SITE 1 1 Schiff-base intermediate with DNA (By
similarity).
ACT_SITE 2 2 Proton donor (By similarity).
ACT_SITE 57 57 Proton donor (in beta-elimination) (By
similarity).
ACT_SITE 262 262 Proton donor (in delta-elimination) (By
similarity).
BINDING 91 91 DNA (By similarity).
BINDING 110 110 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: 273

     PELPEVETVR RGLNRLVSGA TIASIEVFWP KIINNDVDSF KQRLANQTIQ TIDRRGKYLL
     FRFSNGLTMV SHLRMEGKYN VVPRGEDQGK HTHVIFHLTD DRDLLYNDTR KFGRMTLVPT
     GEENTVAGLR TIGPEPVAEQ LTLAYMTATF GKSKKMIKPL LLDQSKIAGI GNIYADETLW
     MSKIHPMRPA NSLTTDEIAT LRQNIIDEMA MAIKGHGTTV HSFSTAFGEA GQFQNHLHVY
     GREGEPCERC GTIIEKIKVA QRGTHFCPLE QRL