ID A0A257W7T8_9BACT Unreviewed; 290 AA.
AC A0A257W7T8;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 08-NOV-2023, entry version 19.
DE RecName: Full=Adenine DNA glycosylase {ECO:0000256|ARBA:ARBA00022023};
DE EC=3.2.2.31 {ECO:0000256|ARBA:ARBA00012045};
DE Flags: Fragment;
GN ORFNames=B7Z55_11025 {ECO:0000313|EMBL:OYW18223.1};
OS Planctomycetales bacterium 12-60-4.
OC Bacteria; Planctomycetota; Planctomycetia; Planctomycetales.
OX NCBI_TaxID=1970541 {ECO:0000313|EMBL:OYW18223.1, ECO:0000313|Proteomes:UP000216774};
RN [1] {ECO:0000313|EMBL:OYW18223.1, ECO:0000313|Proteomes:UP000216774}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12-60-4 {ECO:0000313|EMBL:OYW18223.1};
RA Kantor R.S., Colenbrander Nelson T., Marshall S., Bennett D., Apte S.,
RA Camacho D., Thomas B.C., Warren L.A., Banfield J.F.;
RT "Lifting the veil on microbial sulfur biogeochemistry in mining
RT wastewaters.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolyzes free adenine bases from 7,8-dihydro-8-
CC oxoguanine:adenine mismatched double-stranded DNA, leaving an
CC apurinic site.; EC=3.2.2.31;
CC Evidence={ECO:0000256|ARBA:ARBA00000843};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SIMILARITY: Belongs to the Nth/MutY family.
CC {ECO:0000256|ARBA:ARBA00008343}.
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:OYW18223.1}.
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DR EMBL; NCBX01000730; OYW18223.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A257W7T8; -.
DR Proteomes; UP000216774; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0000701; F:purine-specific mismatch base pair DNA N-glycosylase activity; IEA:UniProtKB-EC.
DR GO; GO:0006284; P:base-excision repair; IEA:InterPro.
DR CDD; cd00056; ENDO3c; 1.
DR Gene3D; 1.10.1670.10; Helix-hairpin-Helix base-excision DNA repair enzymes (C-terminal); 1.
DR Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1.
DR InterPro; IPR011257; DNA_glycosylase.
DR InterPro; IPR004036; Endonuclease-III-like_CS2.
DR InterPro; IPR003265; HhH-GPD_domain.
DR InterPro; IPR023170; HhH_base_excis_C.
DR InterPro; IPR000445; HhH_motif.
DR InterPro; IPR044298; MIG/MutY.
DR InterPro; IPR029119; MutY_C.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR PANTHER; PTHR42944; ADENINE DNA GLYCOSYLASE; 1.
DR PANTHER; PTHR42944:SF1; ADENINE DNA GLYCOSYLASE; 1.
DR Pfam; PF00633; HHH; 1.
DR Pfam; PF00730; HhH-GPD; 1.
DR Pfam; PF14815; NUDIX_4; 1.
DR SMART; SM00478; ENDO3c; 1.
DR SUPFAM; SSF48150; DNA-glycosylase; 1.
DR SUPFAM; SSF55811; Nudix; 1.
DR PROSITE; PS01155; ENDONUCLEASE_III_2; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022485}.
FT DOMAIN 1..164
FT /note="HhH-GPD"
FT /evidence="ECO:0000259|SMART:SM00478"
FT NON_TER 290
FT /evidence="ECO:0000313|EMBL:OYW18223.1"
SQ SEQUENCE 290 AA; 31892 MW; 1A177A1F434A45E1 CRC64;
MLQQTTVAAV IPYFERFLAR FPTLTELAAG EESDVLRLWE GLGYYSRARN LHAAARQIVA
ECDGQFPRDL DELHRLPGIG RYTAGAIASF AFNAPAPIVE ANTQRLYARL LGDDRELKGT
ATQRTLWEFA ALLVGAPSHG RSPSTMEDFG PGAVNQALMD LGATVCTPTA PNCPACPVVR
WCAASAAHRQ HEIPRLAARP VLTDLEDATV AIVDGPRYLL RRRPTGERWA GLWDFPRYTI
PEGQGLSAVV TAGVLQQTGL QISLGPQVAE FKHGVTRYRI TLRCFRGRWN
//
