EX3_SALTI
ID EX3_SALTI Reviewed; 268 AA.
AC P0A1B0; Q9Z612;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Exodeoxyribonuclease III;
DE Short=EXO III;
DE Short=Exonuclease III;
DE EC=3.1.11.2;
DE AltName: Full=AP endonuclease VI;
GN Name=xthA; OrderedLocusNames=STY1812, t1181;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
CC -!- FUNCTION: Major apurinic-apyrimidinic endonuclease of E.coli. It
CC removes the damaged DNA at cytosines and guanines by cleaving on the
CC 3'-side of the AP site by a beta-elimination reaction. It exhibits 3'-
CC 5'-exonuclease, 3'-phosphomonoesterase, 3'-repair diesterase and
CC ribonuclease H activities (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to yield
CC nucleoside 5'-phosphates.; EC=3.1.11.2;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Probably binds two magnesium or manganese ions per subunit.
CC {ECO:0000250};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DNA repair enzymes AP/ExoA family.
CC {ECO:0000305}.
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DR EMBL; AL513382; CAD02052.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO68838.1; -; Genomic_DNA.
DR RefSeq; NP_456210.1; NC_003198.1.
DR RefSeq; WP_000673954.1; NZ_WSUR01000034.1.
DR AlphaFoldDB; P0A1B0; -.
DR SMR; P0A1B0; -.
DR STRING; 220341.16502889; -.
DR PRIDE; P0A1B0; -.
DR EnsemblBacteria; AAO68838; AAO68838; t1181.
DR KEGG; stt:t1181; -.
DR KEGG; sty:STY1812; -.
DR PATRIC; fig|220341.7.peg.1825; -.
DR eggNOG; COG0708; Bacteria.
DR HOGENOM; CLU_027539_0_3_6; -.
DR OMA; WWSYRGR; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0004519; F:endonuclease activity; IEA:InterPro.
DR GO; GO:0008853; F:exodeoxyribonuclease III activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR CDD; cd09086; ExoIII-like_AP-endo; 1.
DR Gene3D; 3.60.10.10; -; 1.
DR InterPro; IPR004808; AP_endonuc_1.
DR InterPro; IPR020847; AP_endonuclease_F1_BS.
DR InterPro; IPR020848; AP_endonuclease_F1_CS.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR InterPro; IPR037493; ExoIII-like.
DR PANTHER; PTHR43250; PTHR43250; 1.
DR Pfam; PF03372; Exo_endo_phos; 1.
DR SUPFAM; SSF56219; SSF56219; 1.
DR TIGRFAMs; TIGR00633; xth; 1.
DR PROSITE; PS00726; AP_NUCLEASE_F1_1; 1.
DR PROSITE; PS00727; AP_NUCLEASE_F1_2; 1.
DR PROSITE; PS00728; AP_NUCLEASE_F1_3; 1.
DR PROSITE; PS51435; AP_NUCLEASE_F1_4; 1.
PE 3: Inferred from homology;
KW DNA damage; DNA repair; Exonuclease; Hydrolase; Magnesium; Metal-binding;
KW Nuclease.
FT CHAIN 1..268
FT /note="Exodeoxyribonuclease III"
FT /id="PRO_0000200023"
FT ACT_SITE 109
FT /evidence="ECO:0000250"
FT ACT_SITE 151
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT BINDING 34
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 151
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 153
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 258
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT SITE 153
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT SITE 229
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT SITE 259
FT /note="Interaction with DNA substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 268 AA; 30785 MW; 6EBBD3E6B481EEE7 CRC64;
MKFVSFNING LRARPHQLEA IVEKHQPDVI GLQETKVHDE MFPLEEVAKL GYNVFYHGQK
GHYGVALLTK ATPISVRRGF PDDGEEAQRR IIMAEIPSPL GNITVINGYF PQGESRDHPL
KFPAKAQFYQ NLQNYLETEL KCDNPVLIMG DMNISPTDLD IGIGEENRKR WLRTGKCSFL
PEEREWMSRL LKWGLVDTFR QANPQTMDKF SWFDYRSKGF VDNRGLRIDL LLASAPLAER
CAETGIDYDI RSMEKPSDHA PVWATFRV
