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Database: UniProt
Entry: A0A1I7GAT6_9BACL
LinkDB: A0A1I7GAT6_9BACL
Original site: A0A1I7GAT6_9BACL 
ID   A0A1I7GAT6_9BACL        Unreviewed;       285 AA.
AC   A0A1I7GAT6;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   08-MAY-2019, entry version 14.
DE   RecName: Full=Formamidopyrimidine-DNA glycosylase {ECO:0000256|HAMAP-Rule:MF_00103};
DE            Short=Fapy-DNA glycosylase {ECO:0000256|HAMAP-Rule:MF_00103};
DE            EC=3.2.2.23 {ECO:0000256|HAMAP-Rule:MF_00103};
DE   AltName: Full=DNA-(apurinic or apyrimidinic site) lyase MutM {ECO:0000256|HAMAP-Rule:MF_00103};
DE            Short=AP lyase MutM {ECO:0000256|HAMAP-Rule:MF_00103};
DE            EC=4.2.99.18 {ECO:0000256|HAMAP-Rule:MF_00103};
GN   Name=mutM {ECO:0000256|HAMAP-Rule:MF_00103};
GN   Synonyms=fpg {ECO:0000256|HAMAP-Rule:MF_00103};
GN   ORFNames=SAMN05421543_102109 {ECO:0000313|EMBL:SFU45567.1};
OS   Alicyclobacillus macrosporangiidus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Alicyclobacillaceae;
OC   Alicyclobacillus.
OX   NCBI_TaxID=392015 {ECO:0000313|EMBL:SFU45567.1, ECO:0000313|Proteomes:UP000183508};
RN   [1] {ECO:0000313|Proteomes:UP000183508}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17980 {ECO:0000313|Proteomes:UP000183508};
RA   Varghese N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in base excision repair of DNA damaged by
CC       oxidation or by mutagenic agents. Acts as DNA glycosylase that
CC       recognizes and removes damaged bases. Has a preference for
CC       oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has
CC       AP (apurinic/apyrimidinic) lyase activity and introduces nicks in
CC       the DNA strand. Cleaves the DNA backbone by beta-delta elimination
CC       to generate a single-strand break at the site of the removed base
CC       with both 3'- and 5'-phosphates. {ECO:0000256|HAMAP-Rule:MF_00103,
CC       ECO:0000256|SAAS:SAAS00411867}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of DNA containing ring-opened 7-methylguanine
CC         residues, releasing 2,6-diamino-4-hydroxy-5-(N-
CC         methyl)formamidopyrimidine.; EC=3.2.2.23;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00103,
CC         ECO:0000256|SAAS:SAAS01116288};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=The C-O-P bond 3' to the apurinic or apyrimidinic site in
CC         DNA is broken by a beta-elimination reaction, leaving a 3'-
CC         terminal unsaturated sugar and a product with a terminal 5'-
CC         phosphate.; EC=4.2.99.18; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00103, ECO:0000256|SAAS:SAAS01121890};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00103};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00103};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00103,
CC       ECO:0000256|SAAS:SAAS00041892}.
CC   -!- SIMILARITY: Belongs to the FPG family. {ECO:0000256|HAMAP-
CC       Rule:MF_00103, ECO:0000256|SAAS:SAAS00557294}.
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DR   EMBL; FPBV01000002; SFU45567.1; -; Genomic_DNA.
DR   RefSeq; WP_074949471.1; NZ_FPBV01000002.1.
DR   STRING; 1382304.JNIL01000001_gene1587; -.
DR   Proteomes; UP000183508; Unassembled WGS sequence.
DR   GO; GO:0140078; F:class I DNA-(apurinic or apyrimidinic site) endonuclease activity; IEA:UniProtKB-EC.
DR   GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR   GO; GO:0008534; F:oxidized purine nucleobase lesion DNA N-glycosylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006284; P:base-excision repair; IEA:InterPro.
DR   GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
DR   Gene3D; 3.20.190.10; -; 1.
DR   HAMAP; MF_00103; Fapy_DNA_glycosyl; 1.
DR   InterPro; IPR015886; DNA_glyclase/AP_lyase_DNA-bd.
DR   InterPro; IPR020629; Formamido-pyr_DNA_Glyclase.
DR   InterPro; IPR012319; FPG_cat.
DR   InterPro; IPR035937; MutM-like_N-ter.
DR   InterPro; IPR010979; Ribosomal_S13-like_H2TH.
DR   InterPro; IPR000214; Znf_DNA_glyclase/AP_lyase.
DR   InterPro; IPR010663; Znf_FPG/IleRS.
DR   Pfam; PF01149; Fapy_DNA_glyco; 1.
DR   Pfam; PF06831; H2TH; 1.
DR   Pfam; PF06827; zf-FPG_IleRS; 1.
DR   SMART; SM00898; Fapy_DNA_glyco; 1.
DR   SMART; SM01232; H2TH; 1.
DR   SUPFAM; SSF46946; SSF46946; 1.
DR   SUPFAM; SSF81624; SSF81624; 1.
DR   TIGRFAMs; TIGR00577; fpg; 1.
DR   PROSITE; PS51068; FPG_CAT; 1.
DR   PROSITE; PS51066; ZF_FPG_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000183508};
KW   DNA damage {ECO:0000256|HAMAP-Rule:MF_00103,
KW   ECO:0000256|SAAS:SAAS01087016};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_00103,
KW   ECO:0000256|SAAS:SAAS01087019};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00103,
KW   ECO:0000256|SAAS:SAAS01087047};
KW   Glycosidase {ECO:0000256|HAMAP-Rule:MF_00103,
KW   ECO:0000256|SAAS:SAAS01087011};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00103,
KW   ECO:0000256|SAAS:SAAS01087030};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00103,
KW   ECO:0000256|SAAS:SAAS01087025};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00103,
KW   ECO:0000256|SAAS:SAAS00551678};
KW   Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_00103,
KW   ECO:0000256|SAAS:SAAS01087023};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00103, ECO:0000256|SAAS:SAAS00551670};
KW   Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00103, ECO:0000256|PROSITE-
KW   ProRule:PRU00391, ECO:0000256|SAAS:SAAS00551733}.
FT   DOMAIN        2    115       FPG_CAT. {ECO:0000259|PROSITE:PS51068}.
FT   DOMAIN      239    273       FPG-type. {ECO:0000259|PROSITE:PS51066}.
FT   ACT_SITE      2      2       Schiff-base intermediate with DNA.
FT                                {ECO:0000256|HAMAP-Rule:MF_00103}.
FT   ACT_SITE      3      3       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00103}.
FT   ACT_SITE     60     60       Proton donor; for beta-elimination
FT                                activity. {ECO:0000256|HAMAP-Rule:
FT                                MF_00103}.
FT   ACT_SITE    263    263       Proton donor; for delta-elimination
FT                                activity. {ECO:0000256|HAMAP-Rule:
FT                                MF_00103}.
FT   BINDING      93     93       DNA. {ECO:0000256|HAMAP-Rule:MF_00103}.
FT   BINDING     112    112       DNA. {ECO:0000256|HAMAP-Rule:MF_00103}.
FT   BINDING     154    154       DNA. {ECO:0000256|HAMAP-Rule:MF_00103}.
SQ   SEQUENCE   285 AA;  31585 MW;  F10CE5FF65E86345 CRC64;
     MPELPEVENV RRDLETLVVG RTVERVDVRL ARIVRTPDDA REFALRLAGC TVTGVRRRGK
     YLLFDVPPYC LVSHLRMEGR YGLAAAHDPE APHTHVVFHF TDGTQLRYRD VRQFGTMDLV
     PAEGPYPAGL AELGPEPFDP ALDPTTFRAR LHHRRAPIKA VLLDQTCVAG LGNIYVDESL
     FLAGIHPERP ASALTRAQCA ALLDAIREIL TRAIDAGGSS VRSYVNGYGR HGGFQMQLNV
     YARAGEPCRR CGTPIEKLRV AGRGTHVCPV CQPAPRRRIR SGRRA
//
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