ID A0A2T6DB27_9BACT Unreviewed; 369 AA.
AC A0A2T6DB27;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE RecName: Full=DNA-(apurinic or apyrimidinic site) lyase {ECO:0000256|ARBA:ARBA00012720};
DE EC=4.2.99.18 {ECO:0000256|ARBA:ARBA00012720};
GN ORFNames=DB346_17495 {ECO:0000313|EMBL:PTX99625.1};
OS Verrucomicrobia bacterium LW23.
OC Bacteria; Verrucomicrobiota.
OX NCBI_TaxID=2161867 {ECO:0000313|EMBL:PTX99625.1, ECO:0000313|Proteomes:UP000244158};
RN [1] {ECO:0000313|EMBL:PTX99625.1, ECO:0000313|Proteomes:UP000244158}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LW23 {ECO:0000313|EMBL:PTX99625.1,
RC ECO:0000313|Proteomes:UP000244158};
RA Buenger W., Mueller J., Hurek T., Reinhold-Hurek B.;
RT "Genomic and phenotypic characterization of four novel plant-associated
RT Verrucomicrobia indicate a new subdivision with one cultivated member.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
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;
CC Evidence={ECO:0000256|ARBA:ARBA00024490};
CC -!- SIMILARITY: Belongs to the type-1 OGG1 family.
CC {ECO:0000256|ARBA:ARBA00010679}.
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:PTX99625.1}.
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DR EMBL; QAZA01000045; PTX99625.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T6DB27; -.
DR OrthoDB; 9798522at2; -.
DR Proteomes; UP000244158; Unassembled WGS sequence.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0008534; F:oxidized purine nucleobase lesion DNA N-glycosylase activity; IEA:InterPro.
DR GO; GO:0006284; P:base-excision repair; IEA:InterPro.
DR GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
DR CDD; cd00056; ENDO3c; 1.
DR Gene3D; 3.30.310.260; -; 1.
DR Gene3D; 1.10.1670.10; Helix-hairpin-Helix base-excision DNA repair enzymes (C-terminal); 1.
DR InterPro; IPR011257; DNA_glycosylase.
DR InterPro; IPR003265; HhH-GPD_domain.
DR InterPro; IPR023170; HhH_base_excis_C.
DR InterPro; IPR012904; OGG_N.
DR PANTHER; PTHR10242; 8-OXOGUANINE DNA GLYCOSYLASE; 1.
DR PANTHER; PTHR10242:SF2; N-GLYCOSYLASE_DNA LYASE; 1.
DR Pfam; PF00730; HhH-GPD; 1.
DR Pfam; PF07934; OGG_N; 1.
DR SMART; SM00478; ENDO3c; 1.
DR SUPFAM; SSF48150; DNA-glycosylase; 1.
DR SUPFAM; SSF55945; TATA-box binding protein-like; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Reference proteome {ECO:0000313|Proteomes:UP000244158}.
FT DOMAIN 191..361
FT /note="HhH-GPD"
FT /evidence="ECO:0000259|SMART:SM00478"
SQ SEQUENCE 369 AA; 40259 MW; 58BCF0CE33AF4E68 CRC64;
MHRYPHRHAN AGRPHAPVTI QRSVSAAPPL HPSTAGDPIA RTAAETLSPF GPVACAELPV
EVMPADLAPF AYDLAITLES GQSFCWRRFP AAAQPGLPQA WIGWAGDIPC VVSQTAPGEQ
LRVIFPSGAA PIESSVAALR TYFQTDTAYT PLLRTFPSAA KDPHLARAMR TCGGMRILRQ
PAWEATASFI CSAQKQILQI MQINAALRRS YADRESDSAR LDHLWPFPHP DALAAQGEEA
LRLCKLGFRA RHLFRTAGQI AAGDPALPSP DAIMELPLPA AVESLTRFHG VGEKVASCIL
LFAYQRTDAF PVDVWIQRIL SNLYIRRKAD AASPEYIRAF ATRHFGPHAG VAQQILFHWY
RTGQAHASG
//