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 01-MAY-2013, entry version 61.
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; Enterobacteriales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2;
RX PubMed=10074092;
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.,
RA Waterston R., Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium
RT 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
CC the 3'-side of the AP site by a beta-elimination reaction. It
CC exhibits 3'-5'-exonuclease, 3'-phosphomonoesterase, 3'-repair
CC diesterase and ribonuclease H activities (By similarity).
CC -!- CATALYTIC ACTIVITY: Exonucleolytic cleavage in the 3'- to 5'-
CC direction to yield nucleoside 5'-phosphates.
CC -!- COFACTOR: Magnesium. Can also utilize manganese. Probably binds
CC two magnesium or manganese ions per subunit (By similarity).
CC -!- SUBUNIT: Monomer (By similarity).
CC -!- SIMILARITY: Belongs to the DNA repair enzymes AP/ExoA family.
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DR EMBL; AF108767; AAD16979.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL20227.1; -; Genomic_DNA.
DR RefSeq; NP_460268.1; NC_003197.1.
DR ProteinModelPortal; P0A1A9; -.
DR SMR; P0A1A9; 1-267.
DR STRING; 99287.STM1302; -.
DR PaxDb; P0A1A9; -.
DR PRIDE; P0A1A9; -.
DR EnsemblBacteria; AAL20227; AAL20227; STM1302.
DR GeneID; 1252820; -.
DR KEGG; stm:STM1302; -.
DR PATRIC; 32381081; VBISalEnt20916_1383.
DR eggNOG; COG0708; -.
DR HOGENOM; HOG000034587; -.
DR KO; K01142; -.
DR OMA; EVNAKRW; -.
DR ProtClustDB; PRK11756; -.
DR GO; GO:0005622; C:intracellular; IEA:InterPro.
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:EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IEA:GOC.
DR InterPro; IPR020847; AP_endonuclease_F1_BS.
DR InterPro; IPR020848; AP_endonuclease_F1_CS.
DR InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR InterPro; IPR004808; ExoDNase_III.
DR PANTHER; PTHR22748; PTHR22748; 1.
DR Pfam; PF03372; Exo_endo_phos; 1.
DR SUPFAM; SSF56219; Exo_endo_phos; 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 Complete proteome; DNA damage; DNA repair; Exonuclease; Hydrolase;
KW Magnesium; Metal-binding; Nuclease; Reference proteome.
FT CHAIN 1 268 Exodeoxyribonuclease III.
FT /FTId=PRO_0000200024.
FT ACT_SITE 109 109 By similarity.
FT ACT_SITE 151 151 Proton donor/acceptor (By similarity).
FT METAL 34 34 Magnesium 1 (By similarity).
FT METAL 151 151 Magnesium 2 (By similarity).
FT METAL 153 153 Magnesium 2 (By similarity).
FT METAL 258 258 Magnesium 1 (By similarity).
FT SITE 153 153 Transition state stabilizer (By
FT similarity).
FT SITE 229 229 Important for catalytic activity (By
FT similarity).
FT SITE 259 259 Interaction with DNA substrate (By
FT similarity).
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
//
