ID G0JU05_9PROT Unreviewed; 270 AA.
AC G0JU05;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 69.
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=Acife_0551 {ECO:0000313|EMBL:AEM46757.1};
OS Acidithiobacillus ferrivorans SS3.
OC Bacteria; Pseudomonadota; Acidithiobacillia; Acidithiobacillales;
OC Acidithiobacillaceae; Acidithiobacillus.
OX NCBI_TaxID=743299 {ECO:0000313|EMBL:AEM46757.1, ECO:0000313|Proteomes:UP000009220};
RN [1] {ECO:0000313|EMBL:AEM46757.1, ECO:0000313|Proteomes:UP000009220}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SS3 {ECO:0000313|EMBL:AEM46757.1,
RC ECO:0000313|Proteomes:UP000009220};
RX PubMed=21705598; DOI=10.1128/JB.05373-11;
RA Liljeqvist M., Valdes J., Holmes D.S., Dopson M.;
RT "Draft genome of the psychrotolerant acidophile Acidithiobacillus
RT ferrivorans SS3.";
RL J. Bacteriol. 193:4304-4305(2011).
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}.
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DR EMBL; CP002985; AEM46757.1; -; Genomic_DNA.
DR RefSeq; WP_014028026.1; NC_015942.1.
DR AlphaFoldDB; G0JU05; -.
DR STRING; 743299.Acife_0551; -.
DR KEGG; afi:Acife_0551; -.
DR eggNOG; COG0266; Bacteria.
DR HOGENOM; CLU_038423_1_1_6; -.
DR Proteomes; UP000009220; Chromosome.
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; IPR015887; DNA_glyclase_Znf_dom_DNA_BS.
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:SF9; ENDONUCLEASE 8-LIKE 1; 1.
DR PANTHER; PTHR22993; 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; PS01242; ZF_FPG_1; 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:UP000009220};
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..113
FT /note="Formamidopyrimidine-DNA glycosylase catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51068"
FT DOMAIN 236..270
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 58
FT /note="Proton donor; for beta-elimination activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00103"
FT ACT_SITE 260
FT /note="Proton donor; for delta-elimination activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00103"
FT BINDING 91
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00103"
FT BINDING 110
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00103"
FT BINDING 151
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00103"
SQ SEQUENCE 270 AA; 30137 MW; 74519010BECF9DE3 CRC64;
MPELPEVEVT RLGIAPHLLG QRLEGAVVRD GRLRLPVNAD LAGRVAGQRL LSLRRRGKYL
LLDLEQGTIL IHLGMSGHLR VLPQSTPVQK HDHVDLLFAD DLCLRFHDPR RFGAVCWLAD
PDQHPFLRHL GPEPLGDDFT AEYLYQRSRS RQVPIKSFLM DAHIVVGVGN IYANESLFAA
GIDPRRHAGM IALQRYGKLV QTVRDILEAA IAQGGTTLRD FTRPDGRNGY FRLSLAVYGR
EGEPCTQCGA LLHGIRISGR ATTYCSHCQR
//
