ID A0A2S8WKD8_9MICC Unreviewed; 335 AA.
AC A0A2S8WKD8;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE RecName: Full=Adenine DNA glycosylase {ECO:0000256|ARBA:ARBA00022023};
DE EC=3.2.2.31 {ECO:0000256|ARBA:ARBA00012045};
GN ORFNames=CQ018_15785 {ECO:0000313|EMBL:PQZ89013.1};
OS Arthrobacter sp. MYb227.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1848601 {ECO:0000313|EMBL:PQZ89013.1, ECO:0000313|Proteomes:UP000239972};
RN [1] {ECO:0000313|EMBL:PQZ89013.1, ECO:0000313|Proteomes:UP000239972}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MYb227 {ECO:0000313|EMBL:PQZ89013.1,
RC ECO:0000313|Proteomes:UP000239972};
RA Zimmermann J., Obeng N., Yang W., Obeng O., Kissoyan K., Pees B.,
RA Dirksen P., Hoppner M., Franke A., Rosenstiel P., Leippe M., Dierking K.,
RA Kaleta C., Schulenburg H.;
RT "Genomic, metabolic, and phenotypic characteristics of bacterial isolates
RT from the natural microbiome of the model nematode Caenorhabditis elegans.";
RL Submitted (SEP-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:PQZ89013.1}.
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DR EMBL; PCPT01000010; PQZ89013.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S8WKD8; -.
DR OrthoDB; 9802365at2; -.
DR Proteomes; UP000239972; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 InterPro; IPR011257; DNA_glycosylase.
DR InterPro; IPR004036; Endonuclease-III-like_CS2.
DR InterPro; IPR003651; Endonuclease3_FeS-loop_motif.
DR InterPro; IPR004035; Endouclease-III_FeS-bd_BS.
DR InterPro; IPR003265; HhH-GPD_domain.
DR InterPro; IPR023170; HhH_base_excis_C.
DR InterPro; IPR000445; HhH_motif.
DR InterPro; IPR044298; MIG/MutY.
DR PANTHER; PTHR42944; ADENINE DNA GLYCOSYLASE; 1.
DR PANTHER; PTHR42944:SF1; ADENINE DNA GLYCOSYLASE; 1.
DR Pfam; PF10576; EndIII_4Fe-2S; 1.
DR Pfam; PF00633; HHH; 1.
DR Pfam; PF00730; HhH-GPD; 1.
DR SMART; SM00478; ENDO3c; 1.
DR SMART; SM00525; FES; 1.
DR SUPFAM; SSF48150; DNA-glycosylase; 1.
DR PROSITE; PS00764; ENDONUCLEASE_III_1; 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:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000239972}.
FT DOMAIN 53..205
FT /note="HhH-GPD"
FT /evidence="ECO:0000259|SMART:SM00478"
SQ SEQUENCE 335 AA; 36529 MW; E01A66F08B8D84C5 CRC64;
MVSHLAIPRI FVPQSALPLL HREIADWYHS NARILPWREE TATPWAIMVS EFMLQQTPVV
RVLPVWEIWM KRWPTPADLA AEPVSEALKA WGRLGYPRRA LRLHAAATLI TEEYAGVVPG
TEAELLALPG VGTYTAAAIA CFAFKEPTVV VDTNIRRVHA RLISGKALPE QNQNAAELAL
AARVLPTNTP LANTWNIGVM ELGALVCTAR SPRCEDCPVM NHCAWIDAGR PEPHYVPKGQ
PWHGTDRQVR GAMMAVLRNS SRPVDRADLL GTPDLGVATG NAQIGALSRV GDPTHEAWVT
LHSLPAELAQ RERALSSLLA DGLAQQAAEG ISLPD
//
