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: 29906
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:
06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
21-DEC-2004, sequence version 2.
07-MAR-2006, entry version 29.
Phylogenetic order:
Bacteria Proteobacteria Gammaproteobacteria Vibrionales Vibrionaceae Vibrio.
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_VIBCH:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | AE004112 | AAF93397.1 | - |
| PIR | G82347 | G82347. | |
| HSSP | P05523 | 1K82 | |
| GenomeReviews | AE003852_GR | VC0221.1 | |
| TIGR | VC0221 | -. | |
| 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=El Tor N16961 / Serotype O1;
RX MEDLINE=20406833; PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A.,
RA Gill S.R., Nelson K.E., Read T.D., Tettelin H., Richardson D.L.,
RA Ermolaeva M.D., Vamathevan J.J., Bass S., Qin H., Dragoi I.,
RA Sellers P., McDonald L.A., Utterback T.R., Fleischmann R.D.,
RA Nierman W.C., White O., Salzberg S.L., Smith H.O., Colwell R.R.,
RA Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
Feature:
INIT_MET 0 0 By similarity.
CHAIN 1 268 Formamidopyrimidine-DNA glycosylase.
/FTId=PRO_0000170882.
ZN_FING 234 268 FPG-type.
ACT_SITE 1 1 Schiff-base intermediate with DNA (By
similarity).
ACT_SITE 2 2 Proton donor (By similarity).
ACT_SITE 56 56 Proton donor (in beta-elimination) (By
similarity).
ACT_SITE 258 258 Proton donor (in delta-elimination) (By
similarity).
BINDING 89 89 DNA (By similarity).
BINDING 108 108 DNA (By similarity).
BINDING 149 149 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: 268
PELPEVEVSR LGISPHLVGG TIQSLVLRTP KLRWPIPQEL KQLEGQTILA IHRRAKYLII
ETAVGSAIVH LGMSGSLRIL DGDFPAAKHD HVDLVMTSGK RLRYNDPRRF GAWLWCAPDE
SHEVLGRLGP EPLTEAFNAE YMMDKARNKR IAVKAFIMDN AAVVGVGNIY ANESLFTSRL
HPLRPAHSLS LEEWQTLVAN IKQVLQVAIK QGGTTLKDFT QSDGKPGYFA QELQVYGKAK
QPCPHCGEPL CEQKIAQRNT FFCPQCQH