ID A5N5D4_CLOK5 Unreviewed; 302 AA.
AC A5N5D4;
DT 10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 10-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=DNA-(apurinic or apyrimidinic site) lyase {ECO:0000256|ARBA:ARBA00012720};
DE EC=4.2.99.18 {ECO:0000256|ARBA:ARBA00012720};
GN OrderedLocusNames=CKL_0461 {ECO:0000313|EMBL:EDK32515.1};
OS Clostridium kluyveri (strain ATCC 8527 / DSM 555 / NCIMB 10680).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=431943 {ECO:0000313|EMBL:EDK32515.1, ECO:0000313|Proteomes:UP000002411};
RN [1] {ECO:0000313|EMBL:EDK32515.1, ECO:0000313|Proteomes:UP000002411}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8527 / DSM 555 / NCIMB 10680
RC {ECO:0000313|Proteomes:UP000002411};
RX PubMed=18218779; DOI=10.1073/pnas.0711093105;
RA Seedorf H., Fricke W.F., Veith B., Brueggemann H., Liesegang H.,
RA Strittmatter A., Miethke M., Buckel W., Hinderberger J., Li F.,
RA Hagemeier C., Thauer R.K., Gottschalk G.;
RT "The genome of Clostridium kluyveri, a strict anaerobe with unique
RT metabolic features.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:2128-2133(2008).
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}.
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DR EMBL; CP000673; EDK32515.1; -; Genomic_DNA.
DR RefSeq; WP_011989030.1; NC_009706.1.
DR AlphaFoldDB; A5N5D4; -.
DR STRING; 431943.CKL_0461; -.
DR KEGG; ckl:CKL_0461; -.
DR eggNOG; COG0122; Bacteria.
DR HOGENOM; CLU_027543_3_0_9; -.
DR Proteomes; UP000002411; Chromosome.
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:UP000002411}.
FT DOMAIN 124..296
FT /note="HhH-GPD"
FT /evidence="ECO:0000259|SMART:SM00478"
SQ SEQUENCE 302 AA; 35513 MW; E119FBF2882AD044 CRC64;
MDFNYIENLQ NGVILKDVRN FELPHIFDCG QCFRWNREKN GNYIGTAFGK VIEVEKKEDD
VFIYNTCEKD FKEIWCEYFD LYRDYGEIKH ILGKDPILKK AVGFGGGIRL LKQEPFELIV
SFIISANNRI PMIKKAIENI SKRWGETLEF KDRVYYAFPK LDRLKEATLE EMEACGTGFR
AKYIVDTISK IYNNGTKSGE SYHEEYDIDW IRMQEDEACH KELQKFMGIG PKVADCIMLF
SMQKYSAFPV DVWVKRAMNH FYLAPDVSLK KIRDFGVDKF GKLSGFAQQY LFYYARENNI
KI
//
