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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: 30688
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 3.
07-MAR-2006, entry version 33.
Phylogenetic order:
Bacteria Deinococcus-Thermus Deinococci Deinococcales Deinococcaceae Deinococcus.
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_DEIRA:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | AE000513 | AAF10070.1 | ALT_INIT |
| HSSP | O50606 | 1EE8 | |
| GenomeReviews | AE000513_GR | DR0493.1 | |
| TIGR | DR0493 | -. | |
| 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=R1 / ATCC 13939 / DSM 20539 / NCIB 9279;
RX MEDLINE=20036896; PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus
RT radiodurans R1.";
RL Science 286:1571-1577(1999).
Feature:
INIT_MET 0 0 By similarity.
CHAIN 1 279 Formamidopyrimidine-DNA glycosylase.
/FTId=PRO_0000170821.
ZN_FING 238 272 FPG-type.
ACT_SITE 1 1 Schiff-base intermediate with DNA (By
similarity).
ACT_SITE 2 2 Proton donor (By similarity).
ACT_SITE 52 52 Proton donor (in beta-elimination) (By
similarity).
ACT_SITE 262 262 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: 279
PELPEVETTR RKIEPLLRGK TIERIVHDAP HRYRNTERAH GRQVRGLTRR GKYLLLHLAA
ADAAEDEPHD LELIVHLGMT GGFRLEEGPH TRVTFELGSG EKLYFNDPRR FGKVVAVAPG
DYASMPTLAA MGPEPLSDDF TEAEFVALAA RCGPVKPWLL SQKPVSGVGN IYADESLWHA
RLHPAQTRLN ADEAGRLYRA IREVMAAAVD KGGSSLGNGV GNYRQHDGEG GGFQHSHHVY
GRAGQPCDRC GTPIEKIVLG QRGTHFCPVC QPLRTDRSA