ID K0DAX6_LEUCJ Unreviewed; 272 AA.
AC K0DAX6;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Exodeoxyribonuclease III {ECO:0000313|EMBL:AFT82010.1};
GN OrderedLocusNames=C270_05505 {ECO:0000313|EMBL:AFT82010.1};
OS Leuconostoc carnosum (strain JB16).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Leuconostoc.
OX NCBI_TaxID=1229758 {ECO:0000313|EMBL:AFT82010.1, ECO:0000313|Proteomes:UP000006299};
RN [1] {ECO:0000313|EMBL:AFT82010.1, ECO:0000313|Proteomes:UP000006299}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JB16 {ECO:0000313|EMBL:AFT82010.1,
RC ECO:0000313|Proteomes:UP000006299};
RX PubMed=23144413; DOI=10.1128/JB.01805-12;
RA Jung J.Y., Lee S.H., Jeon C.O.;
RT "Complete genome sequence of Leuconostoc carnosum strain JB16, isolated
RT from Kimchi.";
RL J. Bacteriol. 194:6672-6673(2012).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR604808-2};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|PIRSR:PIRSR604808-2};
CC Note=Probably binds two magnesium or manganese ions per subunit.
CC {ECO:0000256|PIRSR:PIRSR604808-2};
CC -!- SIMILARITY: Belongs to the DNA repair enzymes AP/ExoA family.
CC {ECO:0000256|ARBA:ARBA00007092}.
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DR EMBL; CP003851; AFT82010.1; -; Genomic_DNA.
DR RefSeq; WP_014974620.1; NC_018673.1.
DR AlphaFoldDB; K0DAX6; -.
DR STRING; 1229758.C270_05505; -.
DR GeneID; 61187559; -.
DR KEGG; lcn:C270_05505; -.
DR PATRIC; fig|1229758.3.peg.1103; -.
DR eggNOG; COG0708; Bacteria.
DR HOGENOM; CLU_027539_1_3_9; -.
DR Proteomes; UP000006299; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0008311; F:double-stranded DNA 3'-5' DNA exonuclease activity; IEA:UniProtKB-EC.
DR GO; GO:0004519; F:endonuclease activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR CDD; cd09087; Ape1-like_AP-endo; 1.
DR Gene3D; 3.60.10.10; Endonuclease/exonuclease/phosphatase; 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 NCBIfam; TIGR00195; exoDNase_III; 1.
DR NCBIfam; TIGR00633; xth; 1.
DR PANTHER; PTHR22748; AP ENDONUCLEASE; 1.
DR PANTHER; PTHR22748:SF6; DNA-(APURINIC OR APYRIMIDINIC SITE) ENDONUCLEASE; 1.
DR Pfam; PF03372; Exo_endo_phos; 1.
DR SUPFAM; SSF56219; DNase I-like; 1.
DR PROSITE; PS00726; AP_NUCLEASE_F1_1; 1.
DR PROSITE; PS00728; AP_NUCLEASE_F1_3; 1.
DR PROSITE; PS51435; AP_NUCLEASE_F1_4; 1.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|PIRSR:PIRSR604808-2};
KW Manganese {ECO:0000256|PIRSR:PIRSR604808-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR604808-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000006299}.
FT DOMAIN 4..245
FT /note="Endonuclease/exonuclease/phosphatase"
FT /evidence="ECO:0000259|Pfam:PF03372"
FT ACT_SITE 125
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-1"
FT ACT_SITE 164
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-1"
FT ACT_SITE 263
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-1"
FT BINDING 7
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2"
FT BINDING 44
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2"
FT BINDING 164
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2"
FT BINDING 166
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2"
FT BINDING 262
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2"
FT BINDING 263
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2"
FT SITE 166
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-3"
FT SITE 237
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-3"
FT SITE 263
FT /note="Interaction with DNA substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-3"
SQ SEQUENCE 272 AA; 30969 MW; 5031E11A19846BAB CRC64;
MQFISWNIDS INAAVEHKSA RGEMTWETLT HIASRQPDVF AIQETKLKNT GMTKKQAEAI
ANLFPDYELY WRSSTARSGY SGTMILSRLK PISVDYPSIG APGDMDQEGR IITLEFENYF
VSTVYTPNSG SSLVRLDDRG MWDNAYRAYI QSLDDQKPVI FSGDMNVAHE EIDLKNPKTN
RHSAGFTDQE REKFSQLLKA GFTDTLRFQN PEIPSIYTWW AQISKTSKIN NSGWRIDYYL
VSNRIANQIA NTGVIDTGAR QDHAPILLEM DF
//
