ID EX3_ECOLI Reviewed; 268 AA.
AC P09030;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 4.
DT 29-MAY-2013, entry version 144.
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; Synonyms=xth; OrderedLocusNames=b1749, JW1738;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=3049539;
RA Saporito S.M., Smith-White B.J., Cunningham R.P.;
RT "Nucleotide sequence of the xth gene of Escherichia coli K-12.";
RL J. Bacteriol. 170:4542-4547(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RA Wurst H., Hoheisel J.D., Pohl F.M.;
RL Submitted (NOV-1988) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M.,
RA Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K.,
RA Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N.,
RA Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J.,
RA Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome
RT corresponding to the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA Mau B., Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1474(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains
RT MG1655 and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP CHARACTERIZATION.
RX PubMed=8948651; DOI=10.1093/nar/24.22.4572;
RA Shida T., Noda M., Sekiguchi J.;
RT "Cleavage of single- and double-stranded DNAs containing an abasic
RT residue by Escherichia coli exonuclease III (AP endonuclease VI).";
RL Nucleic Acids Res. 24:4572-4576(1996).
RN [7]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R.,
RA Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS), AND COFACTOR.
RX PubMed=7885481; DOI=10.1038/374381a0;
RA Mol C.D., Kuo C.-F., Thayer M.M., Cunningham R.P., Tainer J.A.;
RT "Structure and function of the multifunctional DNA-repair enzyme
RT exonuclease III.";
RL Nature 374:381-386(1995).
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.
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.
CC -!- SIMILARITY: Belongs to the DNA repair enzymes AP/ExoA family.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Exonuclease III entry;
CC URL="http://en.wikipedia.org/wiki/Exonuclease_III";
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DR EMBL; X13002; CAA31424.1; -; Genomic_DNA.
DR EMBL; M22592; AAA24767.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74819.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15540.1; -; Genomic_DNA.
DR PIR; E64934; NCECX3.
DR RefSeq; NP_416263.1; NC_000913.2.
DR RefSeq; YP_490010.1; NC_007779.1.
DR PDB; 1AKO; X-ray; 1.70 A; A=1-268.
DR PDBsum; 1AKO; -.
DR ProteinModelPortal; P09030; -.
DR SMR; P09030; 1-268.
DR DIP; DIP-11148N; -.
DR IntAct; P09030; 16.
DR MINT; MINT-1243969; -.
DR STRING; 511145.b1749; -.
DR SWISS-2DPAGE; P09030; -.
DR PaxDb; P09030; -.
DR PRIDE; P09030; -.
DR EnsemblBacteria; AAC74819; AAC74819; b1749.
DR EnsemblBacteria; BAA15540; BAA15540; BAA15540.
DR GeneID; 12932910; -.
DR GeneID; 946254; -.
DR KEGG; ecj:Y75_p1724; -.
DR KEGG; eco:b1749; -.
DR PATRIC; 32118809; VBIEscCol129921_1822.
DR EchoBASE; EB1066; -.
DR EcoGene; EG11073; xthA.
DR eggNOG; COG0708; -.
DR HOGENOM; HOG000034587; -.
DR KO; K01142; -.
DR OMA; EVNAKRW; -.
DR ProtClustDB; PRK11756; -.
DR BioCyc; EcoCyc:EG11073-MONOMER; -.
DR BioCyc; ECOL316407:JW1738-MONOMER; -.
DR BioCyc; MetaCyc:EG11073-MONOMER; -.
DR EvolutionaryTrace; P09030; -.
DR Genevestigator; P09030; -.
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; IDA:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:response to DNA damage stimulus; IDA:EcoCyc.
DR Gene3D; 3.60.10.10; -; 1.
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 1: Evidence at protein level;
KW 3D-structure; Complete proteome; DNA damage; DNA repair; Exonuclease;
KW Hydrolase; Magnesium; Metal-binding; Nuclease; Reference proteome.
FT CHAIN 1 268 Exodeoxyribonuclease III.
FT /FTId=PRO_0000200021.
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).
FT CONFLICT 49 50 KL -> NV (in Ref. 1; AAA24767).
FT STRAND 2 7
FT HELIX 11 13
FT HELIX 15 25
FT STRAND 28 33
FT HELIX 39 41
FT HELIX 44 49
FT STRAND 53 59
FT STRAND 62 71
FT STRAND 74 80
FT HELIX 85 88
FT STRAND 91 98
FT STRAND 101 109
FT HELIX 121 139
FT STRAND 146 151
FT HELIX 158 160
FT HELIX 165 174
FT STRAND 176 179
FT HELIX 181 192
FT STRAND 195 197
FT HELIX 198 202
FT TURN 215 218
FT HELIX 219 222
FT STRAND 229 234
FT HELIX 235 238
FT STRAND 241 246
FT HELIX 248 251
FT STRAND 253 255
FT STRAND 262 266
SQ SEQUENCE 268 AA; 30969 MW; 09E0E263DCF38634 CRC64;
MKFVSFNING LRARPHQLEA IVEKHQPDVI GLQETKVHDD MFPLEEVAKL GYNVFYHGQK
GHYGVALLTK ETPIAVRRGF PGDDEEAQRR IIMAEIPSLL GNVTVINGYF PQGESRDHPI
KFPAKAQFYQ NLQNYLETEL KRDNPVLIMG DMNISPTDLD IGIGEENRKR WLRTGKCSFL
PEEREWMDRL MSWGLVDTFR HANPQTADRF SWFDYRSKGF DDNRGLRIDL LLASQPLAEC
CVETGIDYEI RSMEKPSDHA PVWATFRR
//
