Protein data for FPG_STRPN:

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: 31085

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.
21-DEC-2004, sequence version 2.
07-MAR-2006, entry version 29.

Phylogenetic order:
Bacteria Firmicutes Lactobacillales Streptococcaceae Streptococcus.

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_STRPN:

DatabasePointerAdd. info#1Add. info#2
EMBLAE007401AAK75091.1-
PIRB95112B95112.
HSSPP423711NNJ
GenomeReviewsAE005672_GRSP0970.1
TIGRSP0970-.
BioCycSPNE170187:SP0970-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_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=ATCC BAA-334 / TIGR4;
RX MEDLINE=21357209; PubMed=11463916; DOI=10.1126/science.1061217;
RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T.,
RA Hickey E.K., Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C.,
RA Dougherty B.A., Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT "Complete genome sequence of a virulent isolate of Streptococcus
RT pneumoniae.";
RL Science 293:498-506(2001).

Feature:
INIT_MET 0 0 By similarity.
CHAIN 1 273 Formamidopyrimidine-DNA glycosylase.
/FTId=PRO_0000170869.
ZN_FING 237 271 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 261 261 Proton donor (in delta-elimination) (By
similarity).
BINDING 90 90 DNA (By similarity).
BINDING 109 109 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

     PELPEVETVC RGLEKLIIGK KISSIEIRYP KMIKTDLEEF QRELPSQIIE SMGRRGKYLL
     FYLTDKVLIS HLRMEGKYFY YPDQGPERKH AHVFFHFEDG GTLVYEDVRK FGTMELLVPD
     LLDVYFISKK LGPEPSEQDF DLQVFQSALA KSKKPIKSHL LDQTLVAGLG NIYVDEVLWR
     AQVHPARPSQ TLTAEEATAI HDQTIAVLGQ AVEKGGSTIR TYTNAFGEDG SMQDFHQVYD
     KTGQECVRCG TIIEKIQLGG RGTHFCPNCQ RRD