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: 30903
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:
11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
21-DEC-2004, sequence version 2.
07-MAR-2006, entry version 13.
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_STRA3:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | AL766851 | CAD47213.1 | - |
| HSSP | P42371 | 1NNJ | |
| GenomeReviews | AL732656_GR | gbs1554.1 | |
| SagaList | gbs1554 | -.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=NEM316 / Serotype III;
RX MEDLINE=22242508; PubMed=12354221;
RA Glaser P., Rusniok C., Buchrieser C., Chevalier F., Frangeul L.,
RA Msadek T., Zouine M., Couve E., Lalioui L., Poyart C., Trieu-Cuot P.,
RA Kunst F.;
RT "Genome sequence of Streptococcus agalactiae, a pathogen causing
RT invasive neonatal disease.";
RL Mol. Microbiol. 45:1499-1513(2002).
Feature:
INIT_MET 0 0 By similarity.
CHAIN 1 272 Formamidopyrimidine-DNA glycosylase.
/FTId=PRO_0000170864.
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: 272
PELPEVETVR KGLERLVVNQ EIASITIKVP KMVKTDLNDF MISLPGKTIQ QVLRRGKYLL
FDFGEMVMVS HLRMEGKYLL FPNKVPDNKH FHLYFKLTNG STLVYQDVRK FGTFELVRKS
SLKDYFTQKK LGPEPTADTF QFEPFSKGLA NSKKPIKPLL LDQRLVAGLG NIYVDEVLWA
AKIHPQRLAN QLTESETSLL HKEIIRILTL GIEKGGSTIR TYKNALGEDG TMQKYLQVYG
KTGQPCPRCG CLIKKIKVGG RGTHYCPRCQ CL