ID I9AI61_LACPE Unreviewed; 366 AA.
AC I9AI61;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
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 Name=mutY {ECO:0000313|EMBL:EIW12622.1};
GN ORFNames=KCA1_2732 {ECO:0000313|EMBL:EIW12622.1};
OS Lactiplantibacillus pentosus KCA1.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactiplantibacillus.
OX NCBI_TaxID=1136177 {ECO:0000313|EMBL:EIW12622.1};
RN [1] {ECO:0000313|EMBL:EIW12622.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCA1 {ECO:0000313|EMBL:EIW12622.1};
RX PubMed=23527145;
RA Anukam K.C., Macklaim J.M., Gloor G.B., Reid G., Boekhorst J., Renckens B.,
RA van Hijum S.A., Siezen R.J.;
RT "Genome Sequence of Lactobacillus pentosus KCA1: Vaginal Isolate from a
RT Healthy Premenopausal Woman.";
RL PLoS ONE 8:E59239-E59239(2013).
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:EIW12622.1}.
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DR EMBL; AKAO01000082; EIW12622.1; -; Genomic_DNA.
DR RefSeq; WP_003639941.1; NZ_CM001538.1.
DR AlphaFoldDB; I9AI61; -.
DR PATRIC; fig|1136177.4.peg.2792; -.
DR eggNOG; COG1194; Bacteria.
DR HOGENOM; CLU_012862_0_0_9; -.
DR Proteomes; UP000005826; Chromosome.
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, ECO:0000313|EMBL:EIW12622.1};
KW Iron {ECO:0000256|RuleBase:RU365096}.
FT DOMAIN 44..195
FT /note="HhH-GPD"
FT /evidence="ECO:0000259|SMART:SM00478"
SQ SEQUENCE 366 AA; 41908 MW; 400668BE0A1D6810 CRC64;
MIEWDAATIK DFQTTLLDWF DEEGRDLPWR HDHEPYHVWV SEIMLQQTQV RTVIPYYQRF
MTLFPTIADL AAAPESQLLK AWEGLGYYSR VRNMQRCANQ LLTDYDGQWP RTAAALTDLI
GIGPYTAGAI ASIAFNEPVP AVDGNAYRVF SRLLKIDADI AKPQTRALFE QVISRIIPHD
RPGDFNQAIM DLGSSYMTAR QPDSAHSPVK RFNQAYLDGD ELAYPVKSKK PRPKPIAYVA
VLAQMQDQWL MTKRPSNGML ANLWTVPLIP IEELDLDEDY QPTDLVAAVE TYFKQEYRLT
LTAHYLDKRP VTHTFTHQKW TIQGVGGEVM LSDLAYFAGK TVTTAERQQL PMPKVQEKIF
TRYLSD
//