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Database: UniProt
Entry: A0A2A2AFJ3_9BURK
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ID   A0A2A2AFJ3_9BURK        Unreviewed;       271 AA.
AC   A0A2A2AFJ3;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
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=CK625_06900 {ECO:0000313|EMBL:PAT37330.1};
OS   Vandammella animalimorsus.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Vandammella.
OX   NCBI_TaxID=2029117 {ECO:0000313|EMBL:PAT37330.1, ECO:0000313|Proteomes:UP000218054};
RN   [1] {ECO:0000313|EMBL:PAT37330.1, ECO:0000313|Proteomes:UP000218054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NML00-0135 {ECO:0000313|EMBL:PAT37330.1,
RC   ECO:0000313|Proteomes:UP000218054};
RA   Bernier A.-M., Bernard K.;
RT   "WGS of Clinical strains of the CDC Group NO-1 linked to zoonotic
RT   infections in humans.";
RL   Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in base excision repair of DNA damaged by oxidation
CC       or by mutagenic agents. Acts as DNA glycosylase that recognizes and
CC       removes damaged bases. Has a preference for oxidized purines, such as
CC       7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase
CC       activity and introduces nicks in the DNA strand. Cleaves the DNA
CC       backbone by beta-delta elimination to generate a single-strand break at
CC       the site of the removed base with both 3'- and 5'-phosphates.
CC       {ECO:0000256|HAMAP-Rule:MF_00103}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-
CC         deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-
CC         dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-monophospho-
CC         2'-deoxyribonucleoside-DNA + H(+); Xref=Rhea:RHEA:66592, Rhea:RHEA-
CC         COMP:13180, Rhea:RHEA-COMP:16897, Rhea:RHEA-COMP:17067,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:136412, ChEBI:CHEBI:157695,
CC         ChEBI:CHEBI:167181; EC=4.2.99.18;
CC         Evidence={ECO:0000256|ARBA:ARBA00024490, ECO:0000256|HAMAP-
CC         Rule:MF_00103};
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|ARBA:ARBA00001668, ECO:0000256|HAMAP-
CC         Rule:MF_00103};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00103};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00103};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245, ECO:0000256|HAMAP-
CC       Rule:MF_00103}.
CC   -!- SIMILARITY: Belongs to the FPG family. {ECO:0000256|ARBA:ARBA00009409,
CC       ECO:0000256|HAMAP-Rule:MF_00103}.
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:PAT37330.1}.
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DR   EMBL; NSJB01000003; PAT37330.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A2AFJ3; -.
DR   Proteomes; UP000218054; 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   CDD; cd08966; EcFpg-like_N; 1.
DR   Gene3D; 1.10.8.50; -; 1.
DR   Gene3D; 3.20.190.10; MutM-like, N-terminal; 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_uS13-like_H2TH.
DR   InterPro; IPR000214; Znf_DNA_glyclase/AP_lyase.
DR   InterPro; IPR010663; Znf_FPG/IleRS.
DR   NCBIfam; TIGR00577; fpg; 1.
DR   PANTHER; PTHR22993; FORMAMIDOPYRIMIDINE-DNA GLYCOSYLASE; 1.
DR   PANTHER; PTHR22993:SF9; FORMAMIDOPYRIMIDINE-DNA GLYCOSYLASE; 1.
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; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR   SUPFAM; SSF81624; N-terminal domain of MutM-like DNA repair proteins; 1.
DR   SUPFAM; SSF46946; S13-like H2TH domain; 1.
DR   PROSITE; PS51068; FPG_CAT; 1.
DR   PROSITE; PS51066; ZF_FPG_2; 1.
PE   3: Inferred from homology;
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW   Rule:MF_00103};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW   Rule:MF_00103};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_00103};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|HAMAP-
KW   Rule:MF_00103};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00103};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00103};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00103};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268, ECO:0000256|HAMAP-
KW   Rule:MF_00103}; Reference proteome {ECO:0000313|Proteomes:UP000218054};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00103};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|HAMAP-
KW   Rule:MF_00103}.
FT   DOMAIN          2..111
FT                   /note="Formamidopyrimidine-DNA glycosylase catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51068"
FT   DOMAIN          237..271
FT                   /note="FPG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51066"
FT   ACT_SITE        2
FT                   /note="Schiff-base intermediate with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00103"
FT   ACT_SITE        3
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00103"
FT   ACT_SITE        56
FT                   /note="Proton donor; for beta-elimination activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00103"
FT   ACT_SITE        261
FT                   /note="Proton donor; for delta-elimination activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00103"
FT   BINDING         90
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00103"
FT   BINDING         108
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00103"
FT   BINDING         152
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00103"
SQ   SEQUENCE   271 AA;  28972 MW;  31877E89C70D0F49 CRC64;
     MPELPEVEVT RQGIAPAITG QRIAALVLGK PLRWPLGCAP AALAGRTVQA VRRRGKYLLL
     ELDGPDLLLL HLGMSGSVRI LPLGTPAGPH DHADLVFGHA LLRLHDPRRF GALVYAPSAD
     APIVHKLLGR LGVEPLSEDF TAAHLAAALR GRRVSIKQAL LAGQAVVGVG NIYASEALFL
     AGIDPHTPAG QLRRPRLERL HGAIVQVLNE AVQRGGSSLR DFVASDGSHG HFQLAARVYG
     RQGQPCPRCG AAIRLSTQGQ RSTYHCPRCQ R
//
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