ID F9VIJ9_ARTSS Unreviewed; 291 AA.
AC F9VIJ9;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 43.
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=SFBM_0332 {ECO:0000313|EMBL:BAK56111.1};
OS Arthromitus sp. (strain SFB-mouse-Japan).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Candidatus Arthromitus.
OX NCBI_TaxID=1029718 {ECO:0000313|EMBL:BAK56111.1, ECO:0000313|Proteomes:UP000001636};
RN [1] {ECO:0000313|EMBL:BAK56111.1, ECO:0000313|Proteomes:UP000001636}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SFB-mouse-Japan {ECO:0000313|Proteomes:UP000001636};
RX PubMed=21791478; DOI=10.1093/dnares/dsr022;
RA Kuwahara T., Ogura Y., Oshima K., Kurokawa K., Ooka T., Hirakawa H.,
RA Itoh T., Nakayama-Imaohji H., Ichimura M., Itoh K., Ishifune C.,
RA Maekawa Y., Yasutomo K., Hattori M., Hayashi T.;
RT "The lifestyle of the segmented filamentous bacterium: a non-culturable
RT gut-associated immunostimulating microbe inferred by whole-genome
RT sequencing.";
RL DNA Res. 18:291-303(2011).
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; AP012202; BAK56111.1; -; Genomic_DNA.
DR RefSeq; WP_005807056.1; NC_015913.1.
DR AlphaFoldDB; F9VIJ9; -.
DR STRING; 1029718.SFBM_0332; -.
DR KEGG; asf:SFBM_0332; -.
DR eggNOG; COG0122; Bacteria.
DR HOGENOM; CLU_027543_3_0_9; -.
DR OrthoDB; 9798522at2; -.
DR Proteomes; UP000001636; 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}.
FT DOMAIN 124..285
FT /note="HhH-GPD"
FT /evidence="ECO:0000259|SMART:SM00478"
SQ SEQUENCE 291 AA; 34405 MW; 7ED095CDA7169717 CRC64;
MDFKNYRYLD NKIIVKKTNN FVLKHIFENG QCFRWERTNI GTYIIVAKGR VIELEMDSGD
LLIHNSNVDD FENIWINYFD FERDYCKLKG ELKHDKYLDI AINFGHGLRI LNQDPFEMIL
SFIISSNNRI PMIKKAILSI SEKYGDPISY KGRIYYKFPS LENLANLSQE KFRECSVGFR
DKYLYNTVKL LNEDNDIEYI MNLNDDMCHK ELQKFSGVGS KVSDCIMLFS MKKYSAFPVD
VWVKRAMMKF YVAPDTSLKG IRDFGRELFK DSSGLAQQYL FYYVRENNIK V
//
