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 14.
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_STRA5:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | AE014260 | AAN00356.1 | - |
| HSSP | P42371 | 1NNJ | |
| GenomeReviews | AE009948_GR | SAG1489.1 | |
| TIGR | SAG1489 | -. | |
| 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=2603 V/R / ATCC BAA-611 / Serotype V;
RX MEDLINE=22222988; PubMed=12200547; DOI=10.1073/pnas.182380799;
RA Tettelin H., Masignani V., Cieslewicz M.J., Eisen J.A., Peterson S.N.,
RA Wessels M.R., Paulsen I.T., Nelson K.E., Margarit I., Read T.D.,
RA Madoff L.C., Wolf A.M., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Lewis M.R.,
RA Radune D., Fedorova N.B., Scanlan D., Khouri H.M., Mulligan S.,
RA Carty H.A., Cline R.T., Van Aken S.E., Gill J., Scarselli M., Mora M.,
RA Iacobini E.T., Brettoni C., Galli G., Mariani M., Vegni F., Maione D.,
RA Rinaudo D., Rappuoli R., Telford J.L., Kasper D.L., Grandi G.,
RA Fraser C.M.;
RT "Complete genome sequence and comparative genomic analysis of an
RT emerging human pathogen, serotype V Streptococcus agalactiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:12391-12396(2002).
Feature:
INIT_MET 0 0 By similarity.
CHAIN 1 272 Formamidopyrimidine-DNA glycosylase.
/FTId=PRO_0000170865.
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.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
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