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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: 30960
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 12.
Phylogenetic order:
Bacteria Proteobacteria Gammaproteobacteria Xanthomonadales Xanthomonadaceae Xylella.
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_XYLFA:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | AE003871 | AAF82983.1 | - |
| EMBL | AE003861 | AAF82884.1 | - |
| PIR | G82838 | G82838. | |
| HSSP | P05523 | 1K82 | |
| GenomeReviews | AE003849_GR | Xf0071.1 | |
| GenomeReviews | AE003849_GR | Xf0170.1 | |
| 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 | 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=9a5c;
RX MEDLINE=20365717; PubMed=10910347; DOI=10.1038/35018003;
RA Simpson A.J.G., Reinach F.C., Arruda P., Abreu F.A., Acencio M.,
RA Alvarenga R., Alves L.M.C., Araya J.E., Baia G.S., Baptista C.S.,
RA Barros M.H., Bonaccorsi E.D., Bordin S., Bove J.M., Briones M.R.S.,
RA Bueno M.R.P., Camargo A.A., Camargo L.E.A., Carraro D.M., Carrer H.,
RA Colauto N.B., Colombo C., Costa F.F., Costa M.C.R., Costa-Neto C.M.,
RA Coutinho L.L., Cristofani M., Dias-Neto E., Docena C., El-Dorry H.,
RA Facincani A.P., Ferreira A.J.S., Ferreira V.C.A., Ferro J.A.,
RA Fraga J.S., Franca S.C., Franco M.C., Frohme M., Furlan L.R.,
RA Garnier M., Goldman G.H., Goldman M.H.S., Gomes S.L., Gruber A.,
RA Ho P.L., Hoheisel J.D., Junqueira M.L., Kemper E.L., Kitajima J.P.,
RA Krieger J.E., Kuramae E.E., Laigret F., Lambais M.R., Leite L.C.C.,
RA Lemos E.G.M., Lemos M.V.F., Lopes S.A., Lopes C.R., Machado J.A.,
RA Machado M.A., Madeira A.M.B.N., Madeira H.M.F., Marino C.L.,
RA Marques M.V., Martins E.A.L., Martins E.M.F., Matsukuma A.Y.,
RA Menck C.F.M., Miracca E.C., Miyaki C.Y., Monteiro-Vitorello C.B.,
RA Moon D.H., Nagai M.A., Nascimento A.L.T.O., Netto L.E.S.,
RA Nhani A. Jr., Nobrega F.G., Nunes L.R., Oliveira M.A.,
RA de Oliveira M.C., de Oliveira R.C., Palmieri D.A., Paris A.,
RA Peixoto B.R., Pereira G.A.G., Pereira H.A. Jr., Pesquero J.B.,
RA Quaggio R.B., Roberto P.G., Rodrigues V., de Rosa A.J.M.,
RA de Rosa V.E. Jr., de Sa R.G., Santelli R.V., Sawasaki H.E.,
RA da Silva A.C.R., da Silva A.M., da Silva F.R., Silva W.A. Jr.,
RA da Silveira J.F., Silvestri M.L.Z., Siqueira W.J., de Souza A.A.,
RA de Souza A.P., Terenzi M.F., Truffi D., Tsai S.M., Tsuhako M.H.,
RA Vallada H., Van Sluys M.A., Verjovski-Almeida S., Vettore A.L.,
RA Zago M.A., Zatz M., Meidanis J., Setubal J.C.;
RT "The genome sequence of the plant pathogen Xylella fastidiosa.";
RL Nature 406:151-159(2000).
Feature:
INIT_MET 0 0 By similarity.
CHAIN 1 270 Formamidopyrimidine-DNA glycosylase.
/FTId=PRO_0000170888.
ZN_FING 236 270 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 260 260 Proton donor (in delta-elimination) (By
similarity).
BINDING 91 91 DNA (By similarity).
BINDING 110 110 DNA (By similarity).
BINDING 151 151 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: 270
PELPEVETTL RGLLPYLTNQ LIYSLTLRRR TLRWDIPSHI ESRLPGHRIT TVCRRAKYLL
IDTNAGGSLI IHLGMSGTLR LLAPETPLRP HDHVDIMLNN RRVLRFNDPR RFGCLLWQED
GQIHPLLQRL GCEPLSDSFN GDYLYQCSRA RNVSVKTFLM DQRIVVGVGN IYAAESLFRA
GISPLCEADK ISLQRYRRLA EVVKDILLYA INRGGTTLRD FLSPDGRPGY FKQELFVYGR
QQQPCKQCGS LLRQTTIRQR TTVWCGHCQG