EX3_SALTY
ID EX3_SALTY Reviewed; 268 AA.
AC P0A1A9; Q9Z612;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
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=STM1302;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2;
RX PubMed=10074092; DOI=10.1128/jb.181.6.1934-1938.1999;
RA Lu C.-D., Abdelal A.T.;
RT "Role of ArgR in activation of the ast operon, encoding enzymes of the
RT arginine succinyltransferase pathway in Salmonella typhimurium.";
RL J. Bacteriol. 181:1934-1938(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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; AF108767; AAD16979.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL20227.1; -; Genomic_DNA.
DR RefSeq; NP_460268.1; NC_003197.2.
DR RefSeq; WP_000673954.1; NC_003197.2.
DR AlphaFoldDB; P0A1A9; -.
DR SMR; P0A1A9; -.
DR STRING; 99287.STM1302; -.
DR PaxDb; P0A1A9; -.
DR EnsemblBacteria; AAL20227; AAL20227; STM1302.
DR GeneID; 1252820; -.
DR KEGG; stm:STM1302; -.
DR PATRIC; fig|99287.12.peg.1383; -.
DR HOGENOM; CLU_027539_0_3_6; -.
DR OMA; WWSYRGR; -.
DR PhylomeDB; P0A1A9; -.
DR BioCyc; SENT99287:STM1302-MON; -.
DR Proteomes; UP000001014; 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; Reference proteome.
FT CHAIN 1..268
FT /note="Exodeoxyribonuclease III"
FT /id="PRO_0000200024"
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
