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: 30724
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-OCT-1996, integrated into UniProtKB/Swiss-Prot.
21-DEC-2004, sequence version 3.
07-MAR-2006, entry version 49.
Phylogenetic order:
Bacteria Proteobacteria Betaproteobacteria Neisseriales Neisseriaceae Neisseria.
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_NEIMB:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | U21808 | AAB01505.1 | - |
| EMBL | AE002098 | AAF41671.1 | - |
| PIR | B81099 | B81099. | |
| HSSP | P05523 | 1K82 | |
| GenomeReviews | AE002098_GR | NMB1295.1 | |
| TIGR | NMB1295 | -. | |
| BioCyc | NMEN491:NMB1295-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 [GENOMIC DNA].
RX MEDLINE=96102858; PubMed=8586265; DOI=10.1016/0378-1097(95)00399-5;
RA Swartley J.S., Stephens D.S.;
RT "Co-transcription of a homologue of the formamidopyrimidine-DNA
RT glycosylase (fpg) and lysophosphatidic acid acyltransferase (nlaA) in
RT Neisseria meningitidis.";
RL FEMS Microbiol. Lett. 134:171-176(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC58 / Serogroup B;
RX MEDLINE=20175755; PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C.,
RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F.,
RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D.,
RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D.,
RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E.,
RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M.,
RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M.,
RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R.,
RA Venter J.C.;
RT "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT MC58.";
RL Science 287:1809-1815(2000).
Feature:
INIT_MET 0 0 By similarity.
CHAIN 1 274 Formamidopyrimidine-DNA glycosylase.
/FTId=PRO_0000170843.
ZN_FING 240 274 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 264 264 Proton donor (in delta-elimination) (By
similarity).
BINDING 94 94 DNA (By similarity).
BINDING 113 113 DNA (By similarity).
CONFLICT 60 61 LI -> IV (in Ref. 1).
CONFLICT 65 67 TGV -> KGI (in Ref. 1).
CONFLICT 150 150 A -> V (in Ref. 1).
CONFLICT 212 212 Q -> R (in Ref. 1).
CONFLICT 251 251 R -> Q (in Ref. 1).
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: 274
PELPEVETTL RGIAPHIEGK TVEAVVLRQL KLRWQINPDL GEILSGRQVL SCGRRAKYLL
IRFQTGVLLI HLGMSGSLRI FTPSDGRIGR PDRHDHVDIV FSDGTVMRYR DPRKFGAILW
YEGIEEHHPL LEKLGPEPLS EAFCADYLYA RLKAQKRAVK LALMDNAVVV GVGNIYANES
LFRAGISPHR PANRLKKKEC ALLVETVKAV LQRAIETGGS TLRDFVDSDG KSGYFQQEYT
VYGRHNQPCP RCGGLVVKET LGQRGTFYCP NCQK