ID E6VZD5_PSEA9 Unreviewed; 283 AA.
AC E6VZD5;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Exodeoxyribonuclease III {ECO:0000313|EMBL:ADU64007.1};
DE EC=4.2.99.18 {ECO:0000313|EMBL:ADU64007.1};
GN OrderedLocusNames=Daes_3014 {ECO:0000313|EMBL:ADU64007.1};
OS Pseudodesulfovibrio aespoeensis (strain ATCC 700646 / DSM 10631 / Aspo-2)
OS (Desulfovibrio aespoeensis).
OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC Desulfovibrionaceae.
OX NCBI_TaxID=643562 {ECO:0000313|EMBL:ADU64007.1, ECO:0000313|Proteomes:UP000002191};
RN [1] {ECO:0000313|Proteomes:UP000002191}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700646 / DSM 10631 / Aspo-2
RC {ECO:0000313|Proteomes:UP000002191};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Chertkov O., Misra M., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Ovchinnikova G., Pedersen K., Jagevall S.,
RA Hazen T., Woyke T.;
RT "Complete sequence of Desulfovibrio aespoeensis Aspo-2.";
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADU64007.1, ECO:0000313|Proteomes:UP000002191}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700646 / DSM 10631 / Aspo-2
RC {ECO:0000313|Proteomes:UP000002191};
RX PubMed=24874683;
RA Pedersen K., Bengtsson A., Edlund J., Rabe L., Hazen T., Chakraborty R.,
RA Goodwin L., Shapiro N.;
RT "Complete Genome Sequence of the Subsurface, Mesophilic Sulfate-Reducing
RT Bacterium Desulfovibrio aespoeensis Aspo-2.";
RL Genome Announc. 2:e00509-14(2014).
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; CP002431; ADU64007.1; -; Genomic_DNA.
DR AlphaFoldDB; E6VZD5; -.
DR STRING; 643562.Daes_3014; -.
DR KEGG; das:Daes_3014; -.
DR eggNOG; COG0708; Bacteria.
DR HOGENOM; CLU_027539_1_3_7; -.
DR Proteomes; UP000002191; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008311; F:double-stranded DNA 3'-5' DNA exonuclease activity; IEA:UniProtKB-EC.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR Gene3D; 3.60.10.10; Endonuclease/exonuclease/phosphatase; 1.
DR InterPro; IPR004808; AP_endonuc_1.
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; PS51435; AP_NUCLEASE_F1_4; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:ADU64007.1};
KW Magnesium {ECO:0000256|PIRSR:PIRSR604808-2};
KW Manganese {ECO:0000256|PIRSR:PIRSR604808-2};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR604808-2};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 16..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 32..273
FT /note="Endonuclease/exonuclease/phosphatase"
FT /evidence="ECO:0000259|Pfam:PF03372"
FT ACT_SITE 137
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-1"
FT ACT_SITE 176
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-1"
FT ACT_SITE 273
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-1"
FT BINDING 34
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2"
FT BINDING 62
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2"
FT BINDING 176
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2"
FT BINDING 178
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2"
FT BINDING 272
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2"
FT BINDING 273
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2"
FT SITE 178
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-3"
FT SITE 247
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-3"
FT SITE 273
FT /note="Interaction with DNA substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-3"
SQ SEQUENCE 283 AA; 32528 MW; E05EA261EBF99D9F CRC64;
MQSFCRETGG SKGNRLVRFP FAFGGFGVII YSWNVNGYRA VIKKNFRDWL DGCGGDVVML
QETKAHPDQL APEEREPDSY ANHYWNWSRK KKGYSGVACF ANPEPLAVTI GLPDARFQGE
GRVLHLEYPD FHLFNIYFPN GQMGDDRLAF KMGFYDAFLD HAQALRKTKP IVVGGDFNTA
HCEIDLKNPK ANAERSGFLP EERAWIDRFI AHGYVDTFRL FEDGPGHYSW WSYRFNARQN
NAGWRIDYFF VSEELRPKVV RAWIEPEVPG SDHCPIGVEI DTH
//
