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: 32236
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:
26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
21-DEC-2004, sequence version 2.
07-MAR-2006, entry version 32.
Phylogenetic order:
Bacteria Proteobacteria Alphaproteobacteria Rhizobiales Phyllobacteriaceae Mesorhizobium.
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_RHILO:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | BA000012 | BAB52006.1 | - |
| HSSP | P05523 | 1K82 | |
| GenomeReviews | BA000012_GR | mll5585.1 | |
| BioCyc | MLOT381:MLL5585-MONOMER | -.1 | |
| HAMAP | MF_00103 | - | 1. |
| InterPro | IPR000191 | Fapy_DNA_glyco. | |
| InterPro | IPR012319 | Form_DNAglyc_cat. | |
| InterPro | IPR000214 | Fpg_Zn_BS. | |
| Pfam | PF01149 | Fapy_DNA_glyco | 1. |
| Pfam | PF06831 | H2TH | 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=MAFF303099;
RX MEDLINE=21082930; PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T.,
RA Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Mochizuki Y., Nakayama S., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takeuchi C., Yamada M., Tabata S.;
RT "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT Mesorhizobium loti.";
RL DNA Res. 7:331-338(2000).
Feature:
INIT_MET 0 0 By similarity.
CHAIN 1 295 Formamidopyrimidine-DNA glycosylase.
/FTId=PRO_0000170856.
ZN_FING 259 295 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 285 285 Proton donor (in delta-elimination) (By
similarity).
BINDING 103 103 DNA (By similarity).
BINDING 126 126 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: 295
PELPEVETVR RGLQPVLEGA RLTRVEARRP DLRFPFPERF SERLTGKTIT ALGRRAKYLT
MHVQDGPVLI CHLGMSGSFR IETDDDGETP GVFHHERSKS TAHDHVVFDV VAADGARSRV
IFNDPRRFGF MLFAEGSPET HPMLAGLGVE PTGNTLDGVL LASLLKGRGS PLKAALLDQK
LIAGLGNIYV SEALWRAGLS PLREAGTIAR PSKKARQQSE RLAEAIRSVI SDAIAAGGSS
LRDYMHTDGS LGYFQHSFAV YDREGEPCPK PGCGGHIERV VQSGRSTFYC RTCQS