ID A0A0P6XVF9_9CHLR Unreviewed; 276 AA.
AC A0A0P6XVF9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=ADN01_16240 {ECO:0000313|EMBL:KPL77441.1};
OS Levilinea saccharolytica.
OC Bacteria; Chloroflexota; Anaerolineae; Anaerolineales; Anaerolineaceae;
OC Levilinea.
OX NCBI_TaxID=229921 {ECO:0000313|EMBL:KPL77441.1, ECO:0000313|Proteomes:UP000050501};
RN [1] {ECO:0000313|EMBL:KPL77441.1, ECO:0000313|Proteomes:UP000050501}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIBI-1 {ECO:0000313|EMBL:KPL77441.1,
RC ECO:0000313|Proteomes:UP000050501};
RA Hemp J., Ward L.M., Pace L.A., Fischer W.W.;
RT "Genome sequence of Levilinea saccharolytica DSM 16555.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of DNA containing ring-opened 7-methylguanine
CC residues, releasing 2,6-diamino-4-hydroxy-5-(N-
CC methyl)formamidopyrimidine.; EC=3.2.2.23;
CC Evidence={ECO:0000256|ARBA:ARBA00001668};
CC -!- SIMILARITY: Belongs to the FPG family. {ECO:0000256|ARBA:ARBA00009409}.
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:KPL77441.1}.
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DR EMBL; LGCM01000060; KPL77441.1; -; Genomic_DNA.
DR RefSeq; WP_062419135.1; NZ_LGCM01000060.1.
DR AlphaFoldDB; A0A0P6XVF9; -.
DR STRING; 229921.ADN01_16240; -.
DR PATRIC; fig|229921.5.peg.2682; -.
DR OrthoDB; 9800855at2; -.
DR Proteomes; UP000050501; Unassembled WGS sequence.
DR GO; GO:0140078; F:class I DNA-(apurinic or apyrimidinic site) endonuclease activity; IEA:UniProtKB-EC.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0019104; F:DNA N-glycosylase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006284; P:base-excision repair; IEA:InterPro.
DR Gene3D; 1.10.8.50; -; 1.
DR InterPro; IPR015886; DNA_glyclase/AP_lyase_DNA-bd.
DR InterPro; IPR012319; FPG_cat.
DR InterPro; IPR035937; MutM-like_N-ter.
DR InterPro; IPR010979; Ribosomal_uS13-like_H2TH.
DR PANTHER; PTHR22993:SF9; ENDONUCLEASE 8-LIKE 1; 1.
DR PANTHER; PTHR22993; FORMAMIDOPYRIMIDINE-DNA GLYCOSYLASE; 1.
DR SMART; SM01232; H2TH; 1.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR SUPFAM; SSF81624; N-terminal domain of MutM-like DNA repair proteins; 1.
DR SUPFAM; SSF46946; S13-like H2TH domain; 1.
DR PROSITE; PS51068; FPG_CAT; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Reference proteome {ECO:0000313|Proteomes:UP000050501}.
FT DOMAIN 2..107
FT /note="Formamidopyrimidine-DNA glycosylase catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51068"
SQ SEQUENCE 276 AA; 30072 MW; 2261708A52CB4F6D CRC64;
MIEIPEAATL GHQIREELTG RRVVTVLAGA AAHKFAWYHG DPAGYAPLLE GDTLVSAAAH
GGMLELHTQR ALLLFHDGVN LRLHPAAGPV PGKHQLLLTF DDGSALSASV QMYGGLYAWD
RRETFDNPYY RIALEKPSPL EPEQFTQAYF MQLLAGPDVQ KLSAKAALAT EQRIPGLGNG
VLQDILWKAR LLPRRKISSL TEEEAQKLYV SLMSTLAEMS RLRGRDTEKD LYGIPGGYLT
VMSAKNAGAP CPACGRAIVK EAYMGGSVYT CPNCQH
//
