EX3_HAEIN
ID EX3_HAEIN Reviewed; 267 AA.
AC P44318;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Exodeoxyribonuclease III;
DE Short=EXO III;
DE Short=Exonuclease III;
DE EC=3.1.11.2;
GN Name=xthA; OrderedLocusNames=HI_0041;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
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 (By similarity).
CC {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; L42023; AAC21719.1; -; Genomic_DNA.
DR PIR; H64044; H64044.
DR RefSeq; NP_438214.1; NC_000907.1.
DR RefSeq; WP_005663264.1; NC_000907.1.
DR AlphaFoldDB; P44318; -.
DR SMR; P44318; -.
DR STRING; 71421.HI_0041; -.
DR EnsemblBacteria; AAC21719; AAC21719; HI_0041.
DR KEGG; hin:HI_0041; -.
DR PATRIC; fig|71421.8.peg.41; -.
DR eggNOG; COG0708; Bacteria.
DR HOGENOM; CLU_027539_0_3_6; -.
DR OMA; WWSYRGR; -.
DR PhylomeDB; P44318; -.
DR BioCyc; HINF71421:G1GJ1-41-MON; -.
DR Proteomes; UP000000579; 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..267
FT /note="Exodeoxyribonuclease III"
FT /id="PRO_0000200022"
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 267 AA; 31025 MW; 6B3ADE465A1E347C CRC64;
MKFISFNING LRARPHQLEA IIEKYQPDVI GLQEIKVADE AFPYEITENL GYHVFHHGQK
GHYGVALLTK QEPKVIRRGF PTDNEDAQKR IIMADLETEF GLLTVINGYF PQGESRAHET
KFPAKEKFYA DLQQYLEKEH DKSNPILIMG DMNISPSDLD IGIGDENRKR WLRTGKCSFL
PEERAWYQRL YDYGLEDSFR KLNPTANDKF SWFDYRSKGF DDNRGLRIDH ILVSQKLAER
CVDVGIALDI RAMEKPSDHA PIWAEFK
