ID A0A1I7GTW2_9FIRM Unreviewed; 273 AA.
AC A0A1I7GTW2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
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=SAMN05216540_103100 {ECO:0000313|EMBL:SFU51860.1};
OS Butyrivibrio sp. M55.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Butyrivibrio.
OX NCBI_TaxID=1855323 {ECO:0000313|EMBL:SFU51860.1, ECO:0000313|Proteomes:UP000199511};
RN [1] {ECO:0000313|EMBL:SFU51860.1, ECO:0000313|Proteomes:UP000199511}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M55 {ECO:0000313|EMBL:SFU51860.1,
RC ECO:0000313|Proteomes:UP000199511};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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 ---------------------------------------------------------------------------
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; FPCD01000003; SFU51860.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I7GTW2; -.
DR Proteomes; UP000199511; Unassembled WGS sequence.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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 Lyase {ECO:0000313|EMBL:SFU51860.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199511}.
FT DOMAIN 113..268
FT /note="HhH-GPD"
FT /evidence="ECO:0000259|SMART:SM00478"
SQ SEQUENCE 273 AA; 31314 MW; 20FF322DDBCAF5B2 CRC64;
MKIEIFDDFD LKKIADSGQC FRFNEHGDGY EVTASSKHLF IRKCGEYEYE LDCEPDEYES
FWKDYFDLGL DYRKIRGMID KDTDRYLYDA AEYGKGIRIL KQDPWEMLIS FIISQRKNIP
AIKASIEKLC AAVSREIATD GDGKKIYAFP TPEELAGLSD EKLASCSLGY RDKYVRQAAL
DVASGAVKLD EWGNASDEEL MTGLLGLFGV GVKVANCEIL FGYHRLDAFP KDVWINRVLE
LKYPNGFSFD KYAPYNGIMQ QYLFYYSRNS GLI
//
