ID A0A169ZIA3_9BACL Unreviewed; 385 AA.
AC A0A169ZIA3;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=PGLA_18585 {ECO:0000313|EMBL:OAB39836.1};
OS Paenibacillus glacialis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=494026 {ECO:0000313|EMBL:OAB39836.1, ECO:0000313|Proteomes:UP000076967};
RN [1] {ECO:0000313|EMBL:OAB39836.1, ECO:0000313|Proteomes:UP000076967}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22343 {ECO:0000313|EMBL:OAB39836.1,
RC ECO:0000313|Proteomes:UP000076967};
RA Shin S.-K., Yi H.;
RT "Draft genome sequence of Paenibacillus glacialis DSM 22343.";
RL Submitted (MAR-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}.
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:OAB39836.1}.
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DR EMBL; LVJH01000040; OAB39836.1; -; Genomic_DNA.
DR RefSeq; WP_068535765.1; NZ_LVJH01000040.1.
DR AlphaFoldDB; A0A169ZIA3; -.
DR STRING; 494026.PGLA_18585; -.
DR OrthoDB; 9802365at2; -.
DR Proteomes; UP000076967; 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 42..193
FT /note="HhH-GPD"
FT /evidence="ECO:0000259|SMART:SM00478"
SQ SEQUENCE 385 AA; 44359 MW; 616038D0767A88FF CRC64;
MFNVEQQHYF SENLLRWYLE NRRDLPWRRH RNPYYIWISE IMLQQTRVDT VIPYFNRFIE
RFPTVADLAN APEQDVLKSW EGLGYYSRAR NLQYAAQQVQ DLHGGQVPSD KESVFALKGV
GPYTAGAILS IAFNQPEPAV DGNVMRVLSR FFLIEEDIMK GSTRALMERL VVELIPQGQA
SHFNQALMEL GALVCTPKSP CCLTCPVMEH CEARIEGKES QLPIKSKSKP PRPEQRFVAL
IEGRGNHAGK ILIRQRPDSG LLARMWELPH MISPVSRGGR MADQRAQDLL GAEMVAEGIP
AIPLEHFMDI EHIFSHIRWN LQVYRCKEDQ MLVAENVESV TMDVTDIGDM LTEYRWISEE
DMATYAFPNA FLKMINAHFE EMRMK
//