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Protein data for FPG_BRAJA:

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: 32178

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:
15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
21-DEC-2004, sequence version 2.
07-MAR-2006, entry version 24.

Phylogenetic order:
Bacteria Proteobacteria Alphaproteobacteria Rhizobiales Bradyrhizobiaceae Bradyrhizobium.

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_BRAJA:

DatabasePointerAdd. info#1Add. info#2
EMBLBA000040BAC46027.1-
HSSPP055231K82
GenomeReviewsBA000040_GRblr0762.1
BioCycBJAP224911:BLR0762-MONOMER-.1
HAMAPMF_00103-1.
InterProIPR000191Fapy_DNA_glyco.
InterProIPR012319Form_DNAglyc_cat.
InterProIPR000214Fpg_Zn_BS.
PfamPF01149Fapy_DNA_glyco1.
PfamPF06831H2TH1.
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=USDA 110;
RX MEDLINE=22484998; PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T.,
RA Sasamoto S., Watanabe A., Idesawa K., Iriguchi M., Kawashima K.,
RA Kohara M., Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M.,
RA Tabata S.;
RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT Bradyrhizobium japonicum USDA110.";
RL DNA Res. 9:189-197(2002).

Feature:
INIT_MET 0 0 By similarity.
CHAIN 1 292 Formamidopyrimidine-DNA glycosylase.
/FTId=PRO_0000170814.
ZN_FING 256 292 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 282 282 Proton donor (in delta-elimination) (By
similarity).
BINDING 103 103 DNA (By similarity).
BINDING 122 122 DNA (By similarity).
BINDING 165 165 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: 292

     PELPEVETVR RGLQPVMEGA KIVVAEARRP DLRFPFQPDF VARLQGQVVT GLGRRAKYLM
     ADLASGDVLL MHLGMSGSFR VIKPDNDAAP GEFHYPRGKD TTHDHVLFRM SSGADIVFND
     PRRFGYMKVI ARNALEDEPL LRGLGPEPLG NEFDAAMLAR SCEGKATSLK AALLDQRVVA
     GLGNIYVCEA LHRSHLSPRR IAATLATRKG EPTDHAKRLV GAIHTVLNDA IKAGGSSLRD
     HRQTTGELGY FQHSFKVYDR EGETCKTPAC GGTIKRFTQN GRSTFWCPKC QK

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