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Endonuclease III (EC 4.2.99.18) (DNA-(apurinic or apyrimidinic site) lyase)

 W7QDS2_9ALTE            Unreviewed;       211 AA.
W7QDS2;
16-APR-2014, integrated into UniProtKB/TrEMBL.
16-APR-2014, sequence version 1.
25-OCT-2017, entry version 24.
RecName: Full=Endonuclease III {ECO:0000256|HAMAP-Rule:MF_00942};
EC=4.2.99.18 {ECO:0000256|HAMAP-Rule:MF_00942};
AltName: Full=DNA-(apurinic or apyrimidinic site) lyase {ECO:0000256|HAMAP-Rule:MF_00942};
Name=nth {ECO:0000256|HAMAP-Rule:MF_00942};
ORFNames=DS2_05780 {ECO:0000313|EMBL:EWH11054.1};
Catenovulum agarivorans DS-2.
Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
Alteromonadaceae; Catenovulum.
NCBI_TaxID=1328313 {ECO:0000313|EMBL:EWH11054.1, ECO:0000313|Proteomes:UP000019276};
[1] {ECO:0000313|EMBL:EWH11054.1, ECO:0000313|Proteomes:UP000019276}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=DS-2 {ECO:0000313|EMBL:EWH11054.1,
ECO:0000313|Proteomes:UP000019276};
PubMed=24604650;
Shan D., Li X., Gu Z., Wei G., Gao Z., Shao Z.;
"Draft Genome Sequence of the Agar-Degrading Bacterium Catenovulum sp.
Strain DS-2, Isolated from Intestines of Haliotis diversicolor.";
Genome Announc. 2:e00144-14(2014).
-!- FUNCTION: DNA repair enzyme that has both DNA N-glycosylase
activity and AP-lyase activity. The DNA N-glycosylase activity
releases various damaged pyrimidines from DNA by cleaving the N-
glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The
AP-lyase activity cleaves the phosphodiester bond 3' to the AP
site by a beta-elimination, leaving a 3'-terminal unsaturated
sugar and a product with a terminal 5'-phosphate.
{ECO:0000256|HAMAP-Rule:MF_00942}.
-!- CATALYTIC ACTIVITY: The C-O-P bond 3' to the apurinic or
apyrimidinic site in DNA is broken by a beta-elimination reaction,
leaving a 3'-terminal unsaturated sugar and a product with a
terminal 5'-phosphate. {ECO:0000256|HAMAP-Rule:MF_00942}.
-!- COFACTOR:
Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
Evidence={ECO:0000256|HAMAP-Rule:MF_00942};
Note=Binds 1 [4Fe-4S] cluster. {ECO:0000256|HAMAP-Rule:MF_00942};
-!- SIMILARITY: Belongs to the Nth/MutY family. {ECO:0000256|HAMAP-
Rule:MF_00942}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:EWH11054.1}.
-----------------------------------------------------------------------
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EMBL; ARZY01000007; EWH11054.1; -; Genomic_DNA.
RefSeq; WP_035013724.1; NZ_ARZY01000007.1.
EnsemblBacteria; EWH11054; EWH11054; DS2_05780.
PATRIC; fig|1328313.3.peg.1191; -.
Proteomes; UP000019276; Unassembled WGS sequence.
GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
GO; GO:0140078; F:class I DNA-(apurinic or apyrimidinic site) lyase activity; IEA:UniProtKB-EC.
GO; GO:0140080; F:class III/IV DNA-(apurinic or apyrimidinic site) lyase activity; IEA:UniProtKB-EC.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
GO; GO:0019104; F:DNA N-glycosylase activity; IEA:UniProtKB-UniRule.
GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0006284; P:base-excision repair; IEA:InterPro.
CDD; cd00056; ENDO3c; 1.
Gene3D; 1.10.1670.10; -; 1.
HAMAP; MF_00942; Nth; 1.
InterPro; IPR011257; DNA_glycosylase.
InterPro; IPR004036; Endonuclease-III-like_CS2.
InterPro; IPR003651; Endonuclease3_FeS-loop_motif.
InterPro; IPR004035; Endouclease-III_FeS-bd_BS.
InterPro; IPR003265; HhH-GPD_domain.
InterPro; IPR000445; HhH_motif.
InterPro; IPR023170; HTH_base_excis_C.
InterPro; IPR005759; Nth.
Pfam; PF10576; EndIII_4Fe-2S; 1.
Pfam; PF00633; HHH; 1.
Pfam; PF00730; HhH-GPD; 1.
SMART; SM00478; ENDO3c; 1.
SMART; SM00525; FES; 1.
SUPFAM; SSF48150; SSF48150; 1.
TIGRFAMs; TIGR01083; nth; 1.
PROSITE; PS00764; ENDONUCLEASE_III_1; 1.
PROSITE; PS01155; ENDONUCLEASE_III_2; 1.
3: Inferred from homology;
4Fe-4S {ECO:0000256|HAMAP-Rule:MF_00942};
Complete proteome {ECO:0000313|Proteomes:UP000019276};
DNA damage {ECO:0000256|HAMAP-Rule:MF_00942};
DNA repair {ECO:0000256|HAMAP-Rule:MF_00942};
DNA-binding {ECO:0000256|HAMAP-Rule:MF_00942};
Endonuclease {ECO:0000313|EMBL:EWH11054.1};
Glycosidase {ECO:0000256|HAMAP-Rule:MF_00942};
Hydrolase {ECO:0000256|HAMAP-Rule:MF_00942,
ECO:0000313|EMBL:EWH11054.1}; Iron {ECO:0000256|HAMAP-Rule:MF_00942};
Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_00942};
Lyase {ECO:0000256|HAMAP-Rule:MF_00942};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_00942};
Nuclease {ECO:0000313|EMBL:EWH11054.1};
Reference proteome {ECO:0000313|Proteomes:UP000019276}.
DOMAIN 38 185 ENDO3c. {ECO:0000259|SMART:SM00478}.
METAL 187 187 Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
Rule:MF_00942}.
METAL 194 194 Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
Rule:MF_00942}.
METAL 197 197 Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
Rule:MF_00942}.
METAL 203 203 Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
Rule:MF_00942}.
SEQUENCE 211 AA; 23756 MW; 356880F3E1BF1E47 CRC64;
MNKQKRLEIL QRLRDANPNP TTELEFSTPF ELLVAVTLSA QATDVGVNKA TRKLFPVANT
PEKIIELGLD GLKSYIKTIG LYNSKAENVM KACKMLVEKH NSQVPQSREA LEALPGVGRK
TANVVLNTAF GWPTIAVDTH IFRVSNRTKF AMGKNVDQVE QKLLKVVPKE FKVDVHHWLI
LHGRYTCVAR KPRCGSCIIE DLCEFKEKTE I


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