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Database: UniProt
Entry: D6SB13_FINMA
LinkDB: D6SB13_FINMA
Original site: D6SB13_FINMA 
ID   D6SB13_FINMA            Unreviewed;       297 AA.
AC   D6SB13;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 41.
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=HMPREF0391_11635 {ECO:0000313|EMBL:EFH92663.1};
OS   Finegoldia magna ATCC 53516.
OC   Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC   Finegoldia.
OX   NCBI_TaxID=525282 {ECO:0000313|EMBL:EFH92663.1};
RN   [1] {ECO:0000313|EMBL:EFH92663.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 53516 {ECO:0000313|EMBL:EFH92663.1};
RA   Muzny D., Qin X., Buhay C., Dugan-Rocha S., Ding Y., Chen G., Hawes A.,
RA   Holder M., Jhangiani S., Johnson A., Khan Z., Li Z., Liu W., Liu X.,
RA   Perez L., Shen H., Wang Q., Watt J., Xi L., Xin Y., Zhou J., Deng J.,
RA   Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Villasana D., Johnson A.,
RA   Liu J., Liyanage D., Lorensuhewa L., Robinson T., Song A., Song B.-B.,
RA   Dinh H., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M.,
RA   Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N.,
RA   Okwuonu G., Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W.,
RA   Jakkamsetti A., Pham P., Ruth R., San Lucas F., Warren J., Zhang J.,
RA   Zhao Z., Zhou C., Zhu D., Lee S., Bess C., Blankenburg K., Forbes L.,
RA   Fu Q., Gubbala S., Hirani K., Jayaseelan J.C., Lara F., Munidasa M.,
RA   Palculict T., Patil S., Pu L.-L., Saada N., Tang L., Weissenberger G.,
RA   Zhu Y., Hemphill L., Shang Y., Youmans B., Ayvaz T., Ross M.,
RA   Santibanez J., Aqrawi P., Gross S., Joshi V., Fowler G., Nazareth L.,
RA   Reid J., Worley K., Petrosino J., Highlander S., Gibbs R.;
RL   Submitted (MAY-2010) 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:EFH92663.1}.
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DR   EMBL; ACHM02000003; EFH92663.1; -; Genomic_DNA.
DR   AlphaFoldDB; D6SB13; -.
DR   STRING; 525282.HMPREF0391_11635; -.
DR   eggNOG; COG0122; Bacteria.
DR   HOGENOM; CLU_027543_3_0_9; -.
DR   Proteomes; UP000004063; Chromosome.
DR   GO; GO:0140078; F:class I DNA-(apurinic or apyrimidinic site) endonuclease activity; IEA:RHEA.
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; IPR000445; HhH_motif.
DR   InterPro; IPR012904; OGG_N.
DR   PANTHER; PTHR10242; 8-OXOGUANINE DNA GLYCOSYLASE; 1.
DR   PANTHER; PTHR10242:SF2; N-GLYCOSYLASE_DNA LYASE; 1.
DR   Pfam; PF00633; HHH; 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   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000313|EMBL:EFH92663.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EFH92663.1}.
FT   DOMAIN          127..291
FT                   /note="HhH-GPD"
FT                   /evidence="ECO:0000259|SMART:SM00478"
SQ   SEQUENCE   297 AA;  35002 MW;  E0CBFD7F6102DB29 CRC64;
     MVLMQTQIEF NDELKLTKIK QSSFNPTHIF ECGQAFRWYK EDDMSYTTVD GDMYCNVSLV
     GDYVYIKNCT EDDYYKKWEN YFDLKTDYSK IKEELSFNET LKNALEYGDG IRILNQDKFS
     TIISFIISAN NQIPRIMKSV NLICENYGKL LGEFNGRKLY SFPKPEDLEK VPVEEMREVC
     RVGFRDKRIV DVAKMVADNE FDIFEIDNLS NEELRKELIK LPGVGPKVAD CIMLFSYNRH
     NTFPVDVWIK RVMEYLFIKE ETNKNLIAKY ADDLFGDYAG YAQQYLFYYG RENTIGK
//
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