ID A0A1M5KHM7_9FLAO Unreviewed; 345 AA.
AC A0A1M5KHM7;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Adenine DNA glycosylase {ECO:0000256|ARBA:ARBA00022023, ECO:0000256|RuleBase:RU365096};
DE EC=3.2.2.31 {ECO:0000256|ARBA:ARBA00012045, ECO:0000256|RuleBase:RU365096};
GN ORFNames=SAMN04488116_1590 {ECO:0000313|EMBL:SHG52267.1};
OS Allomuricauda flava.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Allomuricauda.
OX NCBI_TaxID=570519 {ECO:0000313|EMBL:SHG52267.1, ECO:0000313|Proteomes:UP000184532};
RN [1] {ECO:0000313|Proteomes:UP000184532}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22638 {ECO:0000313|Proteomes:UP000184532};
RA Varghese N., Submissions S.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Adenine glycosylase active on G-A mispairs.
CC {ECO:0000256|RuleBase:RU365096}.
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; Evidence={ECO:0000256|ARBA:ARBA00000843,
CC ECO:0000256|RuleBase:RU365096};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|RuleBase:RU365096};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000256|RuleBase:RU365096};
CC -!- SIMILARITY: Belongs to the Nth/MutY family.
CC {ECO:0000256|ARBA:ARBA00008343, ECO:0000256|RuleBase:RU365096}.
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DR EMBL; FQWL01000002; SHG52267.1; -; Genomic_DNA.
DR RefSeq; WP_073178098.1; NZ_FQWL01000002.1.
DR AlphaFoldDB; A0A1M5KHM7; -.
DR STRING; 570519.SAMN04488116_1590; -.
DR OrthoDB; 9802365at2; -.
DR Proteomes; UP000184532; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
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:UniProtKB-UniRule.
DR CDD; cd03431; DNA_Glycosylase_C; 1.
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; IPR005760; A/G_AdeGlyc_MutY.
DR InterPro; IPR011257; DNA_glycosylase.
DR InterPro; IPR003265; HhH-GPD_domain.
DR InterPro; IPR023170; HhH_base_excis_C.
DR InterPro; IPR044298; MIG/MutY.
DR InterPro; IPR029119; MutY_C.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR NCBIfam; TIGR01084; mutY; 1.
DR PANTHER; PTHR42944; ADENINE DNA GLYCOSYLASE; 1.
DR PANTHER; PTHR42944:SF1; ADENINE DNA GLYCOSYLASE; 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.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU365096};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU365096};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Iron {ECO:0000256|RuleBase:RU365096}.
FT DOMAIN 35..186
FT /note="HhH-GPD"
FT /evidence="ECO:0000259|SMART:SM00478"
SQ SEQUENCE 345 AA; 40226 MW; 9F62C2D38FD9A091 CRC64;
MSFSKEILKW YAQNKRPLPW RATKDPYKIW LSEIMLQQTR VAQGMPYYHK FLENFPTVHD
LAKASEERVL KLWQGLGYYS RARNLHATAK MVVDQHLGKF PDTYKALRQL KGVGDYTASA
IASICFDLPE PVVDGNVYRV LARYFGIDLP INSSEGIKYF KTLAREVMDA DEIRDYNQGI
MEFGAMQCAP KSPNCTRCPL NQSCVALKEG KVGELPVKLN KTKVRNRYFN YLVYLNPQRK
TRMEQREGKG IWQNLYQFPL LESDKLLSTD EFVSQLREYE KDLNVGHIVL FNETPIVHKL
SHQHLHTQFW ILEVDEISEE SIPWDKIHDF PVPVLIADFL KTFKI
//
