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Protein data for FPG_ANASP:

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: 31486

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:
19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
21-DEC-2004, sequence version 2.
07-MAR-2006, entry version 27.

Phylogenetic order:
Bacteria Cyanobacteria Nostocales Nostocaceae Nostoc.

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_ANASP:

DatabasePointerAdd. info#1Add. info#2
EMBLBA000019BAB76019.1-
PIRAI2345AI2345.
HSSPP055231K82
GenomeReviewsBA000019_GRalr4320.1
BioCycNOST-PCC-01:NOST-PCC-01-004315-MONOMER-.1
BioCycNSP103690:ALR4320-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].
RX MEDLINE=21595285; PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S.,
RA Watanabe A., Iriguchi M., Ishikawa A., Kawashima K., Kimura T.,
RA Kishida Y., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
RA Nakazaki N., Shimpo S., Sugimoto M., Takazawa M., Yamada M.,
RA Yasuda M., Tabata S.;
RT "Complete genomic sequence of the filamentous nitrogen-fixing
RT cyanobacterium Anabaena sp. strain PCC 7120.";
RL DNA Res. 8:205-213(2001).

Feature:
INIT_MET 0 0 By similarity.
CHAIN 1 282 Formamidopyrimidine-DNA glycosylase.
/FTId=PRO_0000170806.
ZN_FING 248 282 FPG-type.
ACT_SITE 1 1 Schiff-base intermediate with DNA (By
similarity).
ACT_SITE 2 2 Proton donor (By similarity).
ACT_SITE 59 59 Proton donor (in beta-elimination) (By
similarity).
ACT_SITE 272 272 Proton donor (in delta-elimination) (By
similarity).
BINDING 99 99 DNA (By similarity).
BINDING 118 118 DNA (By similarity).
BINDING 163 163 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: 282

     PELPEVETVR RGLNQLTLNR KITGGDVLLH RTIAHPFSVG DFLNGITGST ISTWHRRGKY
     LLAELSASPS TTSIPWLGVH LRMTGQLLWL NQDEPLHKHT RVRIFFEEEQ ELRFVDQRTF
     GQMWWVPPGI AVESVITGLA KLAVDPFSPE FTVEYLANKL HNRRRPIKTA LLDQSVVAGL
     GNIYADEALF KSGVLPETLC TEVQLKQIKL LRTAIIQVLE TSIEAGGTTF SNFLNVKGVN
     GNYGGVAWVY NRAGEPCKVC GDVIQRIKLG GRSSHFCRQC QV

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