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Database: UniProt
Entry: A0A1I5XT06_9FIRM
LinkDB: A0A1I5XT06_9FIRM
Original site: A0A1I5XT06_9FIRM 
ID   A0A1I5XT06_9FIRM        Unreviewed;       360 AA.
AC   A0A1I5XT06;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
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=SAMN02910358_01689 {ECO:0000313|EMBL:SFQ35068.1};
OS   Lachnospiraceae bacterium XBB1006.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX   NCBI_TaxID=1520827 {ECO:0000313|EMBL:SFQ35068.1, ECO:0000313|Proteomes:UP000199554};
RN   [1] {ECO:0000313|EMBL:SFQ35068.1, ECO:0000313|Proteomes:UP000199554}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=XBB1006 {ECO:0000313|EMBL:SFQ35068.1,
RC   ECO:0000313|Proteomes:UP000199554};
RA   de Groot N.N.;
RL   Submitted (OCT-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; FOXT01000011; SFQ35068.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I5XT06; -.
DR   STRING; 1520827.SAMN02910358_01689; -.
DR   OrthoDB; 9802365at2; -.
DR   Proteomes; UP000199554; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199554}.
FT   DOMAIN          42..193
FT                   /note="HhH-GPD"
FT                   /evidence="ECO:0000259|SMART:SM00478"
SQ   SEQUENCE   360 AA;  41037 MW;  6D4AF7159BB79249 CRC64;
     MVTDFSFREI VTPLLVWFDE NKRALPWRED RDAYHIWISE IMLQQTRVQA VIGYYERFME
     RLPNIKSLAE CPEDELMKLW EGLGYYNRAR NLQAAAKTVV ETCDGKMPTT MVELLKLKGI
     GDYTARAIAS QAFEEPVVAV DGNVLRVVTR LSNDDTDIMK QSFRRTVEQR LDAVVPTGRA
     GDFCQALMEL GAIVCVPNAA PQCEQCPLIA YCRAKENDCC MQLPAKRVAK KRRIEERTVF
     ILRTEDAVVL HKRPDSGLLA GLYEFPNALG YMSEKESLNA VCAMGFLPLR IRKMEGAKHI
     FSHVEWHMQG YEVWLDTTAK FPEGTVVANV WQMEEVYSIP AAFEGFKKQI HVVSNTAKKP
//
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