ID A0A366HQI7_9BACT Unreviewed; 217 AA.
AC A0A366HQI7;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Endonuclease III {ECO:0000256|HAMAP-Rule:MF_00942};
DE EC=4.2.99.18 {ECO:0000256|HAMAP-Rule:MF_00942};
DE AltName: Full=DNA-(apurinic or apyrimidinic site) lyase {ECO:0000256|HAMAP-Rule:MF_00942};
GN Name=nth {ECO:0000256|HAMAP-Rule:MF_00942};
GN ORFNames=DES53_102128 {ECO:0000313|EMBL:RBP45746.1};
OS Roseimicrobium gellanilyticum.
OC Bacteria; Verrucomicrobiota; Verrucomicrobiae; Verrucomicrobiales;
OC Verrucomicrobiaceae; Roseimicrobium.
OX NCBI_TaxID=748857 {ECO:0000313|EMBL:RBP45746.1, ECO:0000313|Proteomes:UP000253426};
RN [1] {ECO:0000313|EMBL:RBP45746.1, ECO:0000313|Proteomes:UP000253426}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25532 {ECO:0000313|EMBL:RBP45746.1,
RC ECO:0000313|Proteomes:UP000253426};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: DNA repair enzyme that has both DNA N-glycosylase activity
CC and AP-lyase activity. The DNA N-glycosylase activity releases various
CC damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving
CC an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the
CC phosphodiester bond 3' to the AP site by a beta-elimination, leaving a
CC 3'-terminal unsaturated sugar and a product with a terminal 5'-
CC phosphate. {ECO:0000256|HAMAP-Rule:MF_00942}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-
CC deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-
CC dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-monophospho-
CC 2'-deoxyribonucleoside-DNA + H(+); Xref=Rhea:RHEA:66592, Rhea:RHEA-
CC COMP:13180, Rhea:RHEA-COMP:16897, Rhea:RHEA-COMP:17067,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:136412, ChEBI:CHEBI:157695,
CC ChEBI:CHEBI:167181; EC=4.2.99.18; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_00942};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00942};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000256|HAMAP-Rule:MF_00942};
CC -!- SIMILARITY: Belongs to the Nth/MutY family.
CC {ECO:0000256|ARBA:ARBA00008343, ECO:0000256|HAMAP-Rule:MF_00942}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00942}.
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:RBP45746.1}.
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DR EMBL; QNRR01000002; RBP45746.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A366HQI7; -.
DR OrthoDB; 9800977at2; -.
DR Proteomes; UP000253426; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0140078; F:class I DNA-(apurinic or apyrimidinic site) endonuclease activity; IEA:UniProtKB-EC.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019104; F:DNA N-glycosylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006284; P:base-excision repair; IEA:InterPro.
DR CDD; cd00056; ENDO3c; 1.
DR Gene3D; 1.10.1670.10; Helix-hairpin-Helix base-excision DNA repair enzymes (C-terminal); 1.
DR HAMAP; MF_00942; Nth; 1.
DR InterPro; IPR011257; DNA_glycosylase.
DR InterPro; IPR004036; Endonuclease-III-like_CS2.
DR InterPro; IPR003265; HhH-GPD_domain.
DR InterPro; IPR023170; HhH_base_excis_C.
DR InterPro; IPR000445; HhH_motif.
DR InterPro; IPR005759; Nth.
DR NCBIfam; TIGR01083; nth; 1.
DR PANTHER; PTHR10359; A/G-SPECIFIC ADENINE GLYCOSYLASE/ENDONUCLEASE III; 1.
DR PANTHER; PTHR10359:SF18; ENDONUCLEASE III; 1.
DR Pfam; PF00633; HHH; 1.
DR Pfam; PF00730; HhH-GPD; 1.
DR PIRSF; PIRSF001435; Nth; 1.
DR SMART; SM00478; ENDO3c; 1.
DR SUPFAM; SSF48150; DNA-glycosylase; 1.
DR PROSITE; PS01155; ENDONUCLEASE_III_2; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW Rule:MF_00942};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW Rule:MF_00942}; DNA-binding {ECO:0000256|HAMAP-Rule:MF_00942};
KW Endonuclease {ECO:0000313|EMBL:RBP45746.1};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|HAMAP-
KW Rule:MF_00942};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00942};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Lyase {ECO:0000256|HAMAP-Rule:MF_00942, ECO:0000313|EMBL:RBP45746.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nuclease {ECO:0000313|EMBL:RBP45746.1}.
FT DOMAIN 39..186
FT /note="HhH-GPD"
FT /evidence="ECO:0000259|SMART:SM00478"
SQ SEQUENCE 217 AA; 24373 MW; 6EFA5327D380ACF9 CRC64;
MTKTERAAHV LARLTKLYPE PPIPLDHTDA YTLLIAVLLS AQCTDVRVNL TTPKLFALAR
TPEKMMEVPV EEIQAIIRPC GLSPQKAKAI STLSRILIEK HGGNVPADLE QLEELPGVGH
KTAQVVMAQS FGVPSFPVDT HIHRLAQRWK LSDGKSVTQT ERDLKRLFPK ETWNKLHLQI
IYYGREYCTA RGCDGTVCPI CRELFPERVR AVKTKKA
//
