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Protein data for FPG_MYCGE:

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: 32618

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:
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
21-DEC-2004, sequence version 2.
07-MAR-2006, entry version 43.

Phylogenetic order:
Bacteria Firmicutes Mollicutes Mycoplasmataceae Mycoplasma.

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_MYCGE:

DatabasePointerAdd. info#1Add. info#2
EMBLL43967AAC71484.1-
HSSPP423711NNJ
GenomeReviewsL43967_GRMG262.1.1
TIGRMG262.1-.
BioCycMGEN2097:MG262.1-MONOMER-.1
HAMAPMF_00103-1.
InterProIPR000191Fapy_DNA_glyco.
InterProIPR012319Form_DNAglyc_cat.
InterProIPR000214Fpg_Zn_BS.
PfamPF01149Fapy_DNA_glyco1.
PfamPF06831H2TH1.
ProDomPD003680Fapy_DNA_glyco1.
TIGRFAMsTIGR00577fpg1.
PROSITEPS51068FPG_CAT1.
PROSITEPS01242ZF_FPG_11.
PROSITEPS51066ZF_FPG_21.

General information about the databases mentioned above

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=ATCC 33530 / G-37;
RX MEDLINE=96026346; PubMed=7569993;
RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A.,
RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M.,
RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L.,
RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M.,
RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S.,
RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.;
RT "The minimal gene complement of Mycoplasma genitalium.";
RL Science 270:397-403(1995).
RN [2]
RP IDENTIFICATION.
RX MEDLINE=96239636; PubMed=8638118;
RA Robison K., Gilbert W., Church G.M.;
RT "More Haemophilus and Mycoplasma genes.";
RL Science 271:1302-1303(1996).

Feature:
INIT_MET 0 0 By similarity.
CHAIN 1 283 Formamidopyrimidine-DNA glycosylase.
/FTId=PRO_0000170836.
ZN_FING 238 272 FPG-type.
ACT_SITE 1 1 Schiff-base intermediate with DNA (By
similarity).
ACT_SITE 2 2 Proton donor (By similarity).
ACT_SITE 58 58 Proton donor (in beta-elimination) (By
similarity).
ACT_SITE 262 262 Proton donor (in delta-elimination) (By
similarity).
BINDING 93 93 DNA (By similarity).
BINDING 112 112 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: 283

     PELPEVTTVI NELKETVLNK PLDQVQVNLR KVLKNIDPQL LNKQLKNQFF TDIKRKGKYI
     IFLLSNGLYL VSHLRMEGKY FFEERGSKFN QKHVLVEFHF DDGSQLNYHD TRQFGTFHLY
     EKLEQAAQLN KLAFDPLEAG FDYRKIFQKA QNSKRKVKTF ILDQTVISGI GNIYADEILF
     ASKINPETMV DQLTIKEIEI LCKNATKILA KAIVMKGTTI SSFSFKKDHT GGYQNFLKVH
     TKKDQPCSVC NQLIVKKKIN GRGSYFCLNC QKITTKVSTK LNP

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