ID O51484_BORBU Unreviewed; 255 AA.
AC O51484;
DT 01-JUN-1998, integrated into UniProtKB/TrEMBL.
DT 01-JUN-1998, sequence version 1.
DT 27-MAR-2024, entry version 124.
DE SubName: Full=Exodeoxyribonuclease III {ECO:0000313|EMBL:AAC66902.1};
DE EC=3.1.11.2 {ECO:0000313|EMBL:AAC66902.1};
GN Name=xth {ECO:0000313|EMBL:AAC66902.1};
GN OrderedLocusNames=BB_0534 {ECO:0000313|EMBL:AAC66902.1};
OS Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS (Borrelia burgdorferi).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Borreliaceae;
OC Borreliella.
OX NCBI_TaxID=224326 {ECO:0000313|EMBL:AAC66902.1, ECO:0000313|Proteomes:UP000001807};
RN [1] {ECO:0000313|EMBL:AAC66902.1, ECO:0000313|Proteomes:UP000001807}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35210 / B31 / CIP 102532 / DSM 4680
RC {ECO:0000313|Proteomes:UP000001807};
RX PubMed=9403685; DOI=10.1038/37551;
RA Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R., Lathigra R.,
RA White O., Ketchum K.A., Dodson R., Hickey E.K., Gwinn M., Dougherty B.,
RA Tomb J.F., Fleischmann R.D., Richardson D., Peterson J., Kerlavage A.R.,
RA Quackenbush J., Salzberg S., Hanson M., van Vugt R., Palmer N., Adams M.D.,
RA Gocayne J., Weidman J., Utterback T., Watthey L., McDonald L., Artiach P.,
RA Bowman C., Garland S., Fuji C., Cotton M.D., Horst K., Roberts K.,
RA Hatch B., Smith H.O., Venter J.C.;
RT "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL Nature 390:580-586(1997).
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; AE000783; AAC66902.1; -; Genomic_DNA.
DR PIR; E70166; E70166.
DR RefSeq; NP_212668.1; NC_001318.1.
DR RefSeq; WP_002656039.1; NC_001318.1.
DR AlphaFoldDB; O51484; -.
DR STRING; 224326.BB_0534; -.
DR PaxDb; 224326-BB_0534; -.
DR EnsemblBacteria; AAC66902; AAC66902; BB_0534.
DR GeneID; 56567964; -.
DR KEGG; bbu:BB_0534; -.
DR PATRIC; fig|224326.49.peg.925; -.
DR HOGENOM; CLU_027539_1_3_12; -.
DR OrthoDB; 9803914at2; -.
DR Proteomes; UP000001807; 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; cd09085; Mth212-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; 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; PS51435; AP_NUCLEASE_F1_4; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:AAC66902.1};
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:UP000001807}.
FT DOMAIN 4..243
FT /note="Endonuclease/exonuclease/phosphatase"
FT /evidence="ECO:0000259|Pfam:PF03372"
FT ACT_SITE 106
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-1"
FT ACT_SITE 146
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-1"
FT ACT_SITE 243
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 35
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2"
FT BINDING 146
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2"
FT BINDING 148
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2"
FT BINDING 242
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2"
FT BINDING 243
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2"
FT SITE 148
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-3"
FT SITE 217
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-3"
FT SITE 243
FT /note="Interaction with DNA substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-3"
SQ SEQUENCE 255 AA; 29756 MW; 03C7DDEFD8C9406A CRC64;
MKLISWNVNG IRAVLKKGFL EFVKEYTPDI LCIQETKALR EQLPKDLILE NYYSYFSNSK
IKGYSGVCIY SKVEPISVRL LGEEIFDNEG RGLVACYDDF ILVNGYFPNS QVLRRRLGYK
LDFLSYVENL ADSLVCDGKN VVICGDFNIA HTEIDLISPD SNRDSPGYYI EETTWLDDFL
NKGYVDTFRI FNKDPGYYTW WSYRTRARER NMGWRIDYFI VNEFFKRNVE KSLILDKVMG
SDHCPVFLEL ADVVS
//
