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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: 31522
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:
15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
21-DEC-2004, sequence version 2.
07-MAR-2006, entry version 26.
Phylogenetic order:
Bacteria Firmicutes Bacillales Bacillaceae Bacillus Bacillus cereus group.
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_BACAN:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | AE016879 | AAP28519.1 | - |
| EMBL | AE017334 | AAT33950.1 | - |
| EMBL | AE017225 | AAT56779.1 | - |
| HSSP | P42371 | 1KFV | |
| GenomeReviews | AE016879_GR | BA4830.1 | |
| GenomeReviews | AE017225_GR | BAS4481.1 | |
| GenomeReviews | AE017334_GR | GBAA4830.1 | |
| TIGR | BA4830 | -. | |
| TIGR | GBAA4830 | -. | |
| 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=Ames / isolate Porton;
RX MEDLINE=22608414; PubMed=12721629; DOI=10.1038/nature01586;
RA Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T.,
RA Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R.,
RA Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M.,
RA Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L.,
RA DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H.,
RA Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D.,
RA Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F.,
RA Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C.,
RA Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O.,
RA Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M.,
RA Hanna P.C., Kolstoe A.-B., Fraser C.M.;
RT "The genome sequence of Bacillus anthracis Ames and comparison to
RT closely related bacteria.";
RL Nature 423:81-86(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames ancestor;
RA Ravel J., Rasko D.A., Shumway M.F., Jiang L., Cer R.Z., Federova N.B.,
RA Wilson M., Stanley S., Decker S., Read T.D., Salzberg S.L.,
RA Fraser C.M.;
RT "Bacillus anthracis comparative genomics.";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sterne;
RA Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K.,
RA Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R.,
RA Richardson P., Rubin E., Tice H.;
RT "Complete genome sequence of Bacillus anthracis Sterne.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
Feature:
INIT_MET 0 0 By similarity.
CHAIN 1 275 Formamidopyrimidine-DNA glycosylase.
/FTId=PRO_0000170807.
ZN_FING 239 273 FPG-type.
ACT_SITE 1 1 Schiff-base intermediate with DNA (By
similarity).
ACT_SITE 2 2 Proton donor (By similarity).
ACT_SITE 59 59 Proton donor (in beta-elimination) (By
similarity).
ACT_SITE 263 263 Proton donor (in delta-elimination) (By
similarity).
BINDING 92 92 DNA (By similarity).
BINDING 111 111 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: 275
PELPEVENVR RTLENLVTGK TIEDVIVTYP KIVKRPDDAE IFKEMLKGET IENIKRRGKF
LLLYVTNYVI VSHLRMEGKF LLHQEDEPID KHTHVRFLFT DGTELHYKDV RKFGTMHLFK
KGEEMNQMPL ADLGPEPFDA ELTPQYLHER LQKTNRKIKV VLLDQRLLVG LGNIYVDEVL
FRSQIHPERE ASSLTAEEIE RIYEATVTTL GEAVKRGGST IRTYINSQGQ IGSFQELLNV
YGKKGEPCVT CGTILEKTVV GGRGTHYCPI CQPRI