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: 31517
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:
19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
21-DEC-2004, sequence version 2.
07-MAR-2006, entry version 27.
Phylogenetic order:
Bacteria Actinobacteria Actinobacteridae Actinomycetales Corynebacterineae Corynebacteriaceae Corynebacterium.
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_CORGL:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | BA000036 | BAB99466.1 | - |
| EMBL | BX927154 | CAF20409.1 | ALT_INIT |
| HSSP | P05523 | 1K82 | |
| GenomeReviews | BX927147_GR | cg2272.1 | |
| GenomeReviews | BA000036_GR | Cgl2073.1 | |
| BioCyc | CGLU196627:NCGL1993-MONOMER | -.1 | |
| 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 | 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].
RC STRAIN=ATCC 13032 / DSM 20300 / NCIB 10025;
RA Nakagawa S.;
RT "Complete genomic sequence of Corynebacterium glutamicum ATCC 13032.";
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / NCIB 10025;
RX MEDLINE=22830012; PubMed=12948626; DOI=10.1016/S0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M.,
RA Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L.,
RA Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B.,
RA McHardy A.C., Meyer F., Moeckel B., Pfefferle W., Puehler A.,
RA Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I.,
RA Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence
RT and its impact on the production of L-aspartate-derived amino acids
RT and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
Feature:
INIT_MET 0 0 By similarity.
CHAIN 1 285 Formamidopyrimidine-DNA glycosylase.
/FTId=PRO_0000170820.
ZN_FING 249 283 FPG-type.
ACT_SITE 1 1 Schiff-base intermediate with DNA (By
similarity).
ACT_SITE 2 2 Proton donor (By similarity).
ACT_SITE 60 60 Proton donor (in beta-elimination) (By
similarity).
ACT_SITE 273 273 Proton donor (in delta-elimination) (By
similarity).
BINDING 102 102 DNA (By similarity).
BINDING 121 121 DNA (By similarity).
BINDING 163 163 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: 285
PELPEVEVVR RGLEDHMVGH TIVSATVLHP RAARNQLGGG PEIEANIAGL RVSAAKRRGK
FLWLELIDAP SGETRPDLGL LVHLGMSGQM LIKEPDAPIS PHLRAKVELD NGDEVWFVDQ
RTFGYWWLGD LVDGVPERVS HIATDVLDES ADFSAIARNL KSRKSEIKRL LLNQEIVSGI
GNIYADEMLW QAKIHPLQRA DRLSLARLEE LLQAGKDVMT KALAQGGTSF DALYVNVNGN
SGYFALSLNA YAQTGEPCGR CGTLIIRESF MNRGSHYCPN CQKRR