ID   END3_RICCN              Reviewed;         210 AA.
AC   Q92GH4;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Endonuclease III {ECO:0000255|HAMAP-Rule:MF_00942};
DE            EC=4.2.99.18 {ECO:0000255|HAMAP-Rule:MF_00942};
DE   AltName: Full=DNA-(apurinic or apyrimidinic site) lyase {ECO:0000255|HAMAP-Rule:MF_00942};
GN   Name=nth {ECO:0000255|HAMAP-Rule:MF_00942}; OrderedLocusNames=RC1149;
OS   Rickettsia conorii (strain ATCC VR-613 / Malish 7).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=272944;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-613 / Malish 7;
RX   PubMed=11557893; DOI=10.1126/science.1061471;
RA   Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V.,
RA   Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.;
RT   "Mechanisms of evolution in Rickettsia conorii and R. prowazekii.";
RL   Science 293:2093-2098(2001).
CC   -!- FUNCTION: DNA repair enzyme that has both DNA N-glycosylase activity
CC       and AP-lyase activity. The DNA N-glycosylase activity releases various
CC       damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving
CC       an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the
CC       phosphodiester bond 3' to the AP site by a beta-elimination, leaving a
CC       3'-terminal unsaturated sugar and a product with a terminal 5'-
CC       phosphate. {ECO:0000255|HAMAP-Rule:MF_00942}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-
CC         deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-
CC         dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-monophospho-
CC         2'-deoxyribonucleoside-DNA + H(+); Xref=Rhea:RHEA:66592, Rhea:RHEA-
CC         COMP:13180, Rhea:RHEA-COMP:16897, Rhea:RHEA-COMP:17067,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:136412, ChEBI:CHEBI:157695,
CC         ChEBI:CHEBI:167181; EC=4.2.99.18; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00942};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00942};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000255|HAMAP-Rule:MF_00942};
CC   -!- SIMILARITY: Belongs to the Nth/MutY family. {ECO:0000255|HAMAP-
CC       Rule:MF_00942}.
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DR   EMBL; AE006914; AAL03687.1; -; Genomic_DNA.
DR   PIR; E97843; E97843.
DR   RefSeq; WP_010977720.1; NC_003103.1.
DR   AlphaFoldDB; Q92GH4; -.
DR   SMR; Q92GH4; -.
DR   EnsemblBacteria; AAL03687; AAL03687; RC1149.
DR   KEGG; rco:RC1149; -.
DR   PATRIC; fig|272944.4.peg.1323; -.
DR   HOGENOM; CLU_012862_3_0_5; -.
DR   OMA; QIIWYGR; -.
DR   Proteomes; UP000000816; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0140078; F:class I DNA-(apurinic or apyrimidinic site) endonuclease activity; IEA:UniProtKB-EC.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019104; F:DNA N-glycosylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006284; P:base-excision repair; IEA:InterPro.
DR   CDD; cd00056; ENDO3c; 1.
DR   Gene3D; 1.10.1670.10; -; 1.
DR   HAMAP; MF_00942; Nth; 1.
DR   InterPro; IPR011257; DNA_glycosylase.
DR   InterPro; IPR004036; Endonuclease-III-like_CS2.
DR   InterPro; IPR003651; Endonuclease3_FeS-loop_motif.
DR   InterPro; IPR003265; HhH-GPD_domain.
DR   InterPro; IPR023170; HhH_base_excis_C.
DR   InterPro; IPR000445; HhH_motif.
DR   InterPro; IPR005759; Nth.
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   SUPFAM; SSF48150; SSF48150; 1.
DR   TIGRFAMs; TIGR01083; nth; 1.
DR   PROSITE; PS01155; ENDONUCLEASE_III_2; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; DNA damage; DNA repair; DNA-binding; Glycosidase; Hydrolase; Iron;
KW   Iron-sulfur; Lyase; Metal-binding.
FT   CHAIN           1..210
FT                   /note="Endonuclease III"
FT                   /id="PRO_0000102220"
FT   DOMAIN          108..127
FT                   /note="HhH"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00942"
FT   BINDING         187
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00942"
FT   BINDING         194
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00942"
FT   BINDING         197
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00942"
FT   BINDING         203
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00942"
SQ   SEQUENCE   210 AA;  23702 MW;  1038D894F009EAB1 CRC64;
     MQAQIVNKIF EIFSKNNPNP KTELIYKNDF TLLVAVILSA QATDISVNLA TKSLFATYDT
     PEKILELGEE GLKKYIKSIG LFNSKAKNII ALCKILISNY QASVPNDFKA LIKLPGVGRK
     TANVVLNCLF GMPTMAVDTH VFRVANRIGL AKGDTPEIVE NELLQIIDTK WLTHAHHWLI
     LHGRYICKAR KPDCDICPIK EYCDYYFNLK