ID A0A0Q4QB43_9SPHN Unreviewed; 264 AA.
AC A0A0Q4QB43;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Exodeoxyribonuclease III {ECO:0000313|EMBL:KQN86806.1};
GN ORFNames=ASE90_05790 {ECO:0000313|EMBL:KQN86806.1};
OS Sphingomonas sp. Leaf67.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1736230 {ECO:0000313|EMBL:KQN86806.1, ECO:0000313|Proteomes:UP000051342};
RN [1] {ECO:0000313|EMBL:KQN86806.1, ECO:0000313|Proteomes:UP000051342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf67 {ECO:0000313|EMBL:KQN86806.1,
RC ECO:0000313|Proteomes:UP000051342};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQN86806.1, ECO:0000313|Proteomes:UP000051342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf67 {ECO:0000313|EMBL:KQN86806.1,
RC ECO:0000313|Proteomes:UP000051342};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQN86806.1}.
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DR EMBL; LMLP01000012; KQN86806.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q4QB43; -.
DR STRING; 1736230.ASE90_05790; -.
DR Proteomes; UP000051342; Unassembled WGS sequence.
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; cd09086; ExoIII-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 InterPro; IPR037493; ExoIII-like.
DR NCBIfam; TIGR00633; xth; 1.
DR PANTHER; PTHR43250; EXODEOXYRIBONUCLEASE III; 1.
DR PANTHER; PTHR43250:SF2; EXODEOXYRIBONUCLEASE III; 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 Magnesium {ECO:0000256|PIRSR:PIRSR604808-2};
KW Manganese {ECO:0000256|PIRSR:PIRSR604808-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR604808-2}.
FT DOMAIN 7..255
FT /note="Endonuclease/exonuclease/phosphatase"
FT /evidence="ECO:0000259|Pfam:PF03372"
FT ACT_SITE 108
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-1"
FT ACT_SITE 151
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-1"
FT ACT_SITE 255
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-1"
FT BINDING 10
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2"
FT BINDING 37
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2"
FT BINDING 151
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2"
FT BINDING 153
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2"
FT BINDING 254
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2"
FT BINDING 255
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2"
FT SITE 153
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-3"
FT SITE 225
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-3"
FT SITE 255
FT /note="Interaction with DNA substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-3"
SQ SEQUENCE 264 AA; 30167 MW; DB2B84863E67967F CRC64;
MDTLSVASWN INSVRFRMDI VEQFLREAQP DVLCLQETKV ENRDFPYEPL RRLGYTHIAI
NGQRMHHGVA VISKVPLAED DRLDWQANGE ARHLGVRLAN GLRIENVYIP AGGDVPDRAV
NPKFGQKLDF LERMIEWSHG LSGIPTLLVG DFNVAPLESD VWSHKQLLDV VSHTPIEVAT
LARLQAANDW VDLGRQFVPA PQRLYTWWSY RAKDWAASDR GRRLDHMWAS RDVAAKAVAH
RVHEPCRSWL KPSDHIPIVT EFAF
//
