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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: 31258
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 Proteobacteria Betaproteobacteria Burkholderiales Burkholderiaceae Ralstonia.
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_RALSO:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | AL646059 | CAD13927.1 | - |
| HSSP | P05523 | 1K82 | |
| GenomeReviews | AL646052_GR | RSc0399.1 | |
| BioCyc | RSOL305:RSC0399-MONOMER | -.1 | |
| HAMAP | MF_00103 | - | 1. |
| InterPro | IPR000191 | Fapy_DNA_glyco. | |
| InterPro | IPR012319 | Form_DNAglyc_cat. | |
| InterPro | IPR000214 | Fpg_Zn_BS. | |
| InterPro | IPR010663 | Znf_Fpg. | |
| Pfam | PF01149 | Fapy_DNA_glyco | 1. |
| Pfam | PF06831 | H2TH | 1. |
| Pfam | PF06827 | zf-FPG_IleRS | 1. |
| ProDom | PD003680 | Fapy_DNA_glyco | 1. |
| TIGRFAMs | TIGR00577 | fpg | 1. |
| PROSITE | PS51068 | FPG_CAT | 1. |
| PROSITE | PS01242 | ZF_FPG_1 | 1. |
| PROSITE | PS51066 | ZF_FPG_2 | 1. |
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=GMI1000;
RX MEDLINE=21681879; PubMed=11823852; DOI=10.1038/415497a;
RA Salanoubat M., Genin S., Artiguenave F., Gouzy J., Mangenot S.,
RA Arlat M., Billault A., Brottier P., Camus J.C., Cattolico L.,
RA Chandler M., Choisne N., Claudel-Renard C., Cunnac S., Demange N.,
RA Gaspin C., Lavie M., Moisan A., Robert C., Saurin W., Schiex T.,
RA Siguier P., Thebault P., Whalen M., Wincker P., Levy M.,
RA Weissenbach J., Boucher C.A.;
RT "Genome sequence of the plant pathogen Ralstonia solanacearum.";
RL Nature 415:497-502(2002).
Feature:
INIT_MET 0 0 By similarity.
CHAIN 1 287 Formamidopyrimidine-DNA glycosylase.
/FTId=PRO_0000170855.
ZN_FING 253 287 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 277 277 Proton donor (in delta-elimination) (By
similarity).
BINDING 100 100 DNA (By similarity).
BINDING 123 123 DNA (By similarity).
BINDING 168 168 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: 287
PELPEVEVTR LGLVPHLTGR RIVRAVVRHH GLRWPVDPAL PELLGGRTVA RVLRRGKYLL
IECVPDIAHG PQAGAGWLLV HLGMTGTLRV LETPAAPGTH DHLDIELADA AGRPITLRYR
DPRRFGAVLW HDGDEAALSA HPLLRNLGIE PFDTRFDGDW MYARTRGRSA AIKTVLLAGD
IVVGVGNIYC SESLFRAGIR PTTAAGRISR PRYAALAEAI RATLADAIAR GGSTLRDFVG
SDGQSGYFQL DALVYDRAGL PCRVCGTPIR QIVQGQRSTF YCPACQR