|
|
|
|
|
|
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: 30114
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:
24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
21-DEC-2004, sequence version 2.
07-MAR-2006, entry version 27.
Phylogenetic order:
Bacteria Proteobacteria Gammaproteobacteria Pseudomonadales Pseudomonadaceae Pseudomonas.
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_PSESM:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | AE016853 | AAO53958.1 | - |
| HSSP | P05523 | 1K82 | |
| GenomeReviews | AE016853_GR | PSPTO0414.1 | |
| TIGR | PSPTO0414 | -. | |
| BioCyc | PSYR223283:PSPTO0414-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 | FALSE_NEG. |
| 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=DC3000;
RX MEDLINE=22834015; PubMed=12928499; DOI=10.1073/pnas.1731982100;
RA Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T.,
RA Gwinn M.L., Dodson R.J., DeBoy R.T., Durkin A.S., Kolonay J.F.,
RA Madupu R., Daugherty S.C., Brinkac L.M., Beanan M.J., Haft D.H.,
RA Nelson W.C., Davidsen T.M., Zafar N., Zhou L., Liu J., Yuan Q.,
RA Khouri H.M., Fedorova N.B., Tran B., Russell D., Berry K.J.,
RA Utterback T.R., Van Aken S.E., Feldblyum T.V., D'Ascenzo M.,
RA Deng W.-L., Ramos A.R., Alfano J.R., Cartinhour S., Chatterjee A.K.,
RA Delaney T.P., Lazarowitz S.G., Martin G.B., Schneider D.J., Tang X.,
RA Bender C.L., White O., Fraser C.M., Collmer A.;
RT "The complete genome sequence of the Arabidopsis and tomato pathogen
RT Pseudomonas syringae pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(2003).
Feature:
INIT_MET 0 0 By similarity.
CHAIN 1 269 Formamidopyrimidine-DNA glycosylase.
/FTId=PRO_0000170854.
ZN_FING 235 269 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 259 259 Proton donor (in delta-elimination) (By
similarity).
BINDING 90 90 DNA (By similarity).
BINDING 109 109 DNA (By similarity).
BINDING 150 150 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: 269
PELPEVETTR RGIAPHLEGQ RVSRVIVRDG RLRWPVPEDL DIRLSGQRIV QVSRRAKYLL
IQAEVGTLIS HLGMSGNLRL VEAGLAALKH EHVDIELESG LALRYTDPRR FGAMLWSHDP
HNHELLIRLG PEPLTDLFDG ERLYERSRGK SIAVKPFIMD NAVVVGVGNI YATEALFAAG
IDPRREARGI SRARYLKLAI EIKRILAYAI ERGGTTLRDF IGGDGKPGYF QQELFAYGRG
GQPCKVCGTT LREIKLGQRA SVYCPKCQR