ID   END3_ECOL6              Reviewed;         211 AA.
AC   P0AB84; P20625;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   16-JUN-2009, entry version 32.
DE   RecName: Full=Endonuclease III;
DE            EC=4.2.99.18;
DE   AltName: Full=DNA-(apurinic or apyrimidinic site) lyase;
GN   Name=nth; OrderedLocusNames=c2025;
OS   Escherichia coli O6.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=217992;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O6:H1 / CFT073 / ATCC 700928 / UPEC;
RX   MEDLINE=22388234; PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P.,
RA   Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D.,
RA   Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T.,
RA   Mobley H.L.T., Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence
RT   of uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: Has both an apurinic and/or apyrimidinic endonuclease
CC       activity and a DNA N-glycosylase activity. Incises damaged DNA at
CC       cytosines, thymines and guanines. Acts on a damaged strand, 5'
CC       from the damaged site. Required for the repair of both oxidative
CC       DNA damage and spontaneous mutagenic lesions (By similarity).
CC   -!- CATALYTIC ACTIVITY: The C-O-P bond 3' to the apurinic or
CC       apyrimidinic site in DNA is broken by a beta-elimination reaction,
CC       leaving a 3'-terminal unsaturated sugar and a product with a
CC       terminal 5'-phosphate.
CC   -!- COFACTOR: Binds 1 4Fe-4S cluster. The cluster is not important for
CC       the catalytic activity, but which is probably involved in the
CC       proper positioning of the enzyme along the DNA strand (By
CC       similarity).
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SIMILARITY: Belongs to the nth/mutY family.
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DR   EMBL; AE014075; AAN80485.1; -; Genomic_DNA.
DR   RefSeq; NP_753920.1; -.
DR   SMR; P0AB84; 1-211.
DR   GeneID; 1036116; -.
DR   GenomeReviews; AE014075_GR; c2025.
DR   KEGG; ecc:c2025; -.
DR   HOGENOM; P0AB84; -.
DR   OMA; P0AB84; EPTIAVD.
DR   BRENDA; 4.2.99.18; 292881.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) lyase a...; IEA:EC.
DR   GO; GO:0004519; F:endonuclease activity; IEA:InterPro.
DR   GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006284; P:base-excision repair; IEA:InterPro.
DR   InterPro; IPR004036; Endonuclease-III_CS2.
DR   InterPro; IPR005759; Endonuclease-III_Nth.
DR   InterPro; IPR004035; Endouclease-III_FeS-bd_CS1.
DR   InterPro; IPR003651; Endouclease3-like_FeS-loop.
DR   InterPro; IPR003583; Helix-hairpin-helix_DNA-bd.
DR   InterPro; IPR003265; HhH-GPD_domain.
DR   InterPro; IPR000445; HhH_motif.
DR   Pfam; PF10576; EndIII_4Fe-2S; 1.
DR   Pfam; PF00633; HHH; 1.
DR   Pfam; PF00730; HhH-GPD; 1.
DR   SMART; SM00478; ENDO3c; 1.
DR   SMART; SM00525; FES; 1.
DR   SMART; SM00278; HhH1; 1.
DR   TIGRFAMs; TIGR01083; nth; 1.
DR   PROSITE; PS00764; ENDONUCLEASE_III_1; 1.
DR   PROSITE; PS01155; ENDONUCLEASE_III_2; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Complete proteome; DNA damage; DNA repair; Glycosidase;
KW   Hydrolase; Iron; Iron-sulfur; Lyase; Metal-binding.
FT   CHAIN         1    211       Endonuclease III.
FT                                /FTId=PRO_0000102211.
FT   ACT_SITE    112    112       Nucleophile; for N-glycosylase activity
FT                                (By similarity).
FT   METAL       187    187       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       194    194       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       197    197       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       203    203       Iron-sulfur (4Fe-4S).
SQ   SEQUENCE   211 AA;  23562 MW;  FF4245823B7F902B CRC64;
     MNKAKRLEIL TRLRENNPHP TTELNFSSPF ELLIAVLLSA QATDVSVNKA TAKLYPVANT
     PAAMLELGVE GVKTYIKTIG LYNSKAENII KTCRILLEQH NGEVPEDRAA LEALPGVGRK
     TANVVLNTAF GWPTIAVDTH IFRVCNRTQF APGKNVEQVE EKLLKVVPAE FKVDCHHWLI
     LHGRYTCIAR KPRCGSCIIE DLCEYKEKVD I
//