ID Q2S025_SALRD Unreviewed; 324 AA.
AC Q2S025;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 114.
DE RecName: Full=Endonuclease III {ECO:0000256|HAMAP-Rule:MF_00942};
DE EC=4.2.99.18 {ECO:0000256|HAMAP-Rule:MF_00942};
DE AltName: Full=DNA-(apurinic or apyrimidinic site) lyase {ECO:0000256|HAMAP-Rule:MF_00942};
GN Name=nth {ECO:0000256|HAMAP-Rule:MF_00942,
GN ECO:0000313|EMBL:ABC45958.1};
GN OrderedLocusNames=SRU_2356 {ECO:0000313|EMBL:ABC45958.1};
OS Salinibacter ruber (strain DSM 13855 / M31).
OC Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Salinibacteraceae;
OC Salinibacter.
OX NCBI_TaxID=309807 {ECO:0000313|EMBL:ABC45958.1, ECO:0000313|Proteomes:UP000008674};
RN [1] {ECO:0000313|EMBL:ABC45958.1, ECO:0000313|Proteomes:UP000008674}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13855 / CECT 5946 / M31
RC {ECO:0000313|Proteomes:UP000008674};
RX PubMed=16330755; DOI=10.1073/pnas.0509073102;
RA Mongodin E.F., Nelson K.E., Daugherty S., Deboy R.T., Wister J., Khouri H.,
RA Weidman J., Walsh D.A., Papke R.T., Sanchez Perez G., Sharma A.K.,
RA Nesbo C.L., MacLeod D., Bapteste E., Doolittle W.F., Charlebois R.L.,
RA Legault B., Rodriguez-Valera F.;
RT "The genome of Salinibacter ruber: convergence and gene exchange among
RT hyperhalophilic bacteria and archaea.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:18147-18152(2005).
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:0000256|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:0000256|HAMAP-
CC Rule:MF_00942};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00942};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000256|HAMAP-Rule:MF_00942};
CC -!- SIMILARITY: Belongs to the Nth/MutY family.
CC {ECO:0000256|ARBA:ARBA00008343, ECO:0000256|HAMAP-Rule:MF_00942}.
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DR EMBL; CP000159; ABC45958.1; -; Genomic_DNA.
DR RefSeq; YP_446456.1; NC_007677.1.
DR AlphaFoldDB; Q2S025; -.
DR STRING; 309807.SRU_2356; -.
DR EnsemblBacteria; ABC45958; ABC45958; SRU_2356.
DR KEGG; sru:SRU_2356; -.
DR PATRIC; fig|309807.25.peg.2454; -.
DR eggNOG; COG0177; Bacteria.
DR HOGENOM; CLU_012862_3_3_10; -.
DR OrthoDB; 9800977at2; -.
DR Proteomes; UP000008674; 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:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
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; Helix-hairpin-Helix base-excision DNA repair enzymes (C-terminal); 1.
DR HAMAP; MF_00942; Nth; 1.
DR InterPro; IPR011257; DNA_glycosylase.
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 NCBIfam; TIGR01083; nth; 1.
DR PANTHER; PTHR10359; A/G-SPECIFIC ADENINE GLYCOSYLASE/ENDONUCLEASE III; 1.
DR PANTHER; PTHR10359:SF18; ENDONUCLEASE III; 1.
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; DNA-glycosylase; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_00942};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW Rule:MF_00942};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW Rule:MF_00942}; DNA-binding {ECO:0000256|HAMAP-Rule:MF_00942};
KW Endonuclease {ECO:0000313|EMBL:ABC45958.1};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|HAMAP-
KW Rule:MF_00942};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00942};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_00942};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW Rule:MF_00942};
KW Lyase {ECO:0000256|HAMAP-Rule:MF_00942, ECO:0000313|EMBL:ABC45958.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00942}; Nuclease {ECO:0000313|EMBL:ABC45958.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008674}.
FT DOMAIN 81..230
FT /note="HhH-GPD"
FT /evidence="ECO:0000259|SMART:SM00478"
FT BINDING 232
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00942"
FT BINDING 239
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00942"
FT BINDING 242
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00942"
FT BINDING 248
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00942"
SQ SEQUENCE 324 AA; 36506 MW; 23D33520BEC7A14D CRC64;
METEGAMGHD VKHWANWSRL ERSPAPWVQR ADVIFEPAHP SPVGRSDRAD VVLEELRERI
DRPTTELQYD TPYQLLVAVI LSAQCTDERV NKATPDLFDA YPAVEALAEA TPDDIHPYIQ
SITFPNNKAG YLARMARQVV DNFDGKVPET IDDLETLTGV GRKTARVVAQ VAHDADALPV
DTHVFRVANR IGLVKEDATT PKKVEQQLKR VIPKAEWGEA HHLLILHGRY TCTARSPDCH
DCPIHEECKH YDRLQRLPDP IDGLDSSAGT YYCTTSDHYF DDPETHVDRY DLEQVACPRC
GSMQVVRTST GEPTKQVKDY RVNG
//
