ID U2BDN4_CLOSY Unreviewed; 293 AA.
AC U2BDN4;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=CLOSYM_02746 {ECO:0000313|EMBL:ERI76224.1};
OS [Clostridium] symbiosum ATCC 14940.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=411472 {ECO:0000313|EMBL:ERI76224.1, ECO:0000313|Proteomes:UP000016491};
RN [1] {ECO:0000313|EMBL:ERI76224.1, ECO:0000313|Proteomes:UP000016491}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14940 {ECO:0000313|EMBL:ERI76224.1,
RC ECO:0000313|Proteomes:UP000016491};
RA Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R., Fronick C.,
RA O'Laughlin M., Godfrey J., Miner T., Herter B., Appelbaum E., Cordes M.,
RA Lek S., Wollam A., Pepin K.H., Palsikar V.B., Mitreva M., Wilson R.K.;
RL Submitted (JUL-2013) 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:ERI76224.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AWSU01000212; ERI76224.1; -; Genomic_DNA.
DR RefSeq; WP_009297889.1; NZ_KE993009.1.
DR AlphaFoldDB; U2BDN4; -.
DR PATRIC; fig|411472.5.peg.2590; -.
DR HOGENOM; CLU_027543_3_0_9; -.
DR Proteomes; UP000016491; 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}.
FT DOMAIN 111..285
FT /note="HhH-GPD"
FT /evidence="ECO:0000259|SMART:SM00478"
SQ SEQUENCE 293 AA; 34023 MW; 0B23175E1671326B CRC64;
MITIEINHFD LRQIAGSGQC FRMNCLEPGL YSAVSRGRYL EISQEGQQFH FHCPDEDYPF
WHHYFDLNTD YGAFLSSVKK RDHYLQNAAN AGSGIRILNQ DAWEMIITFI ISQQRTIPKI
REAVENLSRL YGEEKHCTFP GGKTVVYFSF PTPAQLKKAS LEDLQSLKLG YRARYIHRIC
LDADNGTLDL NRLSAMGYRD AMEYLSGFYG IGTKVANCIC LFGLHHIEAF PVDTWIQQIL
TNHYYRKKYD ALPKSRLYET MVQENFGKYK GYAGVMQQYI FYYERTVLHG RSS
//
