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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: 32565
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 3.
07-MAR-2006, entry version 46.
Phylogenetic order:
Bacteria Proteobacteria Alphaproteobacteria Rhizobiales Rhizobiaceae Sinorhizobium.
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_RHIME:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | AL591783 | CAC41802.1 | - |
| EMBL | L39265 | AAA91094.1 | - |
| HSSP | P05523 | 1K82 | |
| GenomeReviews | AL591688_GR | R00365.1 | |
| BioCyc | SMEL382:SMC01154-MONOMER | -.1 | |
| 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 | 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=1021;
RX MEDLINE=21396507; PubMed=11481430; DOI=10.1073/pnas.161294398;
RA Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J.,
RA Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S.,
RA Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D.,
RA Pohl T., Portetelle D., Puehler A., Purnelle B., Ramsperger U.,
RA Renard C., Thebault P., Vandenbol M., Weidner S., Galibert F.;
RT "Analysis of the chromosome sequence of the legume symbiont
RT Sinorhizobium meliloti strain 1021.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 231-300.
RC STRAIN=1021;
RX MEDLINE=95270610; PubMed=7751302;
RA Margolin W., Bramhill D., Long S.R.;
RT "The dnaA gene of Rhizobium meliloti lies within an unusual gene
RT arrangement.";
RL J. Bacteriol. 177:2892-2900(1995).
Feature:
INIT_MET 0 0 By similarity.
CHAIN 1 300 Formamidopyrimidine-DNA glycosylase.
/FTId=PRO_0000170857.
ZN_FING 264 300 FPG-type.
ACT_SITE 1 1 Schiff-base intermediate with DNA (By
similarity).
ACT_SITE 2 2 Proton donor (By similarity).
ACT_SITE 57 57 Proton donor (in beta-elimination) (By
similarity).
ACT_SITE 290 290 Proton donor (in delta-elimination) (By
similarity).
BINDING 108 108 DNA (By similarity).
BINDING 130 130 DNA (By similarity).
BINDING 173 173 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: 300
PELPEVETVK RGLAPTMEGA LLVRAELRRP DLRFPFPENF ANAVAGRRII ALSRRAKYLM
IELEGGDVII AHLGMSGSFR IEKGPIEAGA DPATPGAFHH PRGKDEKHDH VVFHLDGGSG
PARVIYNDPR RFGFMDLARR SALADHVFLR GLGEEPTGNA LDAAYLATRF AGKIQPLKAA
LLDQRTIAGL GNIYVCEALW RSGLSPKRSA GTLVDKRGRP KQALIALTER IRAVIADAIA
AGGSSLKDHI QADGSLGYFQ HSFSVYDREG EACRTPGCHG TVARIVQAGR STFYCPHCQK