|
|
|
|
|
|
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: 32530
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-JUL-2002, integrated into UniProtKB/Swiss-Prot.
21-DEC-2004, sequence version 3.
07-MAR-2006, entry version 29.
Phylogenetic order:
Bacteria Proteobacteria Alphaproteobacteria Rhizobiales Rhizobiaceae Agrobacterium.
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_AGRT5:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | AE009003 | AAL41343.1 | - |
| EMBL | AE007970 | AAK86137.1 | ALT_INIT |
| PIR | AI2615 | AI2615. | |
| HSSP | P05523 | 1K82 | |
| GenomeReviews | AE007869_GR | AGR_C_561.1 | |
| GenomeReviews | AE008688_GR | Atu0321.1 | |
| 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].
RX MEDLINE=21608550; PubMed=11743193; DOI=10.1126/science.1066804;
RA Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P.,
RA Okura V.K., Zhou Y., Chen L., Wood G.E., Almeida N.F. Jr., Woo L.,
RA Chen Y., Paulsen I.T., Eisen J.A., Karp P.D., Bovee D. Sr.,
RA Chapman P., Clendenning J., Deatherage G., Gillet W., Grant C.,
RA Kutyavin T., Levy R., Li M.-J., McClelland E., Palmieri A.,
RA Raymond C., Rouse G., Saenphimmachak C., Wu Z., Romero P., Gordon D.,
RA Zhang S., Yoo H., Tao Y., Biddle P., Jung M., Krespan W., Perry M.,
RA Gordon-Kamm B., Liao L., Kim S., Hendrick C., Zhao Z.-Y., Dolan M.,
RA Chumley F., Tingey S.V., Tomb J.-F., Gordon M.P., Olson M.V.,
RA Nester E.W.;
RT "The genome of the natural genetic engineer Agrobacterium tumefaciens
RT C58.";
RL Science 294:2317-2323(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX MEDLINE=21608551; PubMed=11743194; DOI=10.1126/science.1066803;
RA Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M.,
RA Qurollo B., Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L.,
RA Houmiel K., Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F.,
RA Wollam C., Allinger M., Doughty D., Scott C., Lappas C., Markelz B.,
RA Flanagan C., Crowell C., Gurson J., Lomo C., Sear C., Strub G.,
RA Cielo C., Slater S.;
RT "Genome sequence of the plant pathogen and biotechnology agent
RT Agrobacterium tumefaciens C58.";
RL Science 294:2323-2328(2001).
Feature:
INIT_MET 0 0 By similarity.
CHAIN 1 297 Formamidopyrimidine-DNA glycosylase.
/FTId=PRO_0000170805.
ZN_FING 261 297 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 287 287 Proton donor (in delta-elimination) (By
similarity).
BINDING 105 105 DNA (By similarity).
BINDING 127 127 DNA (By similarity).
BINDING 170 170 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: 297
PELPEVETVR RGLAPAMEGA RVRKLHLGRP DLRFPFPADF AGLIEGKTII SLGRRAKYLL
IELEDGLTIV SHLGMSGSFR IEAEKGEGGE APGAFHYARS KDGKHDHVVF HLDKGEERVC
VIYNDPRRFG FMHLVERNKL DLYPAFAELG PEPTGNALSA DYLASRFEGK SQPLKSTLLD
QKIIAGLGNI YVCEALWRAH LSPLRAAGTL VTTRGKPKAQ LIDLTEKIRD VIADAIAAGG
SSLRDHIQTD GTLGYFQHSF SVYDQEGQPC RTPGCGGTVE RVVQAGRSTF YCAACQK