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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: 31930
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 45.
Phylogenetic order:
Bacteria Cyanobacteria Chroococcales Synechocystis.
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_SYNY3:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | BA000022 | BAA18384.1 | - |
| EMBL | J05079 | AAA88630.1 | ALT_FRAME |
| PIR | S75925 | S75925. | |
| HSSP | P42371 | 1KFV | |
| GenomeReviews | BA000022_GR | slr1689.1 | |
| BioCyc | SSP1148:SLR1689-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].
RX MEDLINE=97061201; PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T.,
RA Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S.,
RA Shimpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M.,
RA Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the
RT entire genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-168.
RX MEDLINE=90036928; PubMed=2509456;
RA Chitnis P.R., Reilly P.A., Miedel M.C., Nelson N.;
RT "Structure and targeted mutagenesis of the gene encoding 8-kDa subunit
RT of photosystem I from the cyanobacterium Synechocystis sp. PCC 6803.";
RL J. Biol. Chem. 264:18374-18380(1989).
Feature:
INIT_MET 0 0 By similarity.
CHAIN 1 286 Formamidopyrimidine-DNA glycosylase.
/FTId=PRO_0000170879.
ZN_FING 248 282 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 272 272 Proton donor (in delta-elimination) (By
similarity).
BINDING 99 99 DNA (By similarity).
BINDING 118 118 DNA (By similarity).
CONFLICT 128 129 GD -> AI (in Ref. 2).
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.
-!- CAUTION: Ref.2 sequence differs from that shown due to a
frameshift in position 37.
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Sequence length: 286
PELPEVETVC RGLNRLTLEQ TIGGGEVLLD RSLAYPVSVE DFQKQITGCR LVGWQRRGKY
LLGELRSNQA PGPAGWLGCH LRMTGQLLWT ERDQQRPRHT RVVLHFEGGW ELRFVDTRTF
GKVWLLPGDR PWAEVMTGLG QLGPEPFGAD FTAEYLYEKL KSSRRPLKNA LLDQRLVAGL
GNIYADEVLF FCGFHPTMAS NQVSLQDCEL IHQQIQATLT AAIEAGGTSF SDYRQVTGIN
GNYGGMAQVY GREGEPCRHC GTVIAKIKLG GRSAHFCPQC QPKLER