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Database: UniProt
Entry: A0A076HXW7_9BACT
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ID   A0A076HXW7_9BACT        Unreviewed;       276 AA.
AC   A0A076HXW7;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=DNA-formamidopyrimidine glycosylase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=N008_15995 {ECO:0000313|EMBL:AII53472.1};
OS   Hymenobacter sp. APR13.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC   Hymenobacter.
OX   NCBI_TaxID=1356852 {ECO:0000313|EMBL:AII53472.1, ECO:0000313|Proteomes:UP000028590};
RN   [1] {ECO:0000313|EMBL:AII53472.1, ECO:0000313|Proteomes:UP000028590}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APR13 {ECO:0000313|EMBL:AII53472.1,
RC   ECO:0000313|Proteomes:UP000028590};
RA   Li P., Jiang J., Kwok A.H.Y., Lou X., Xu D., Leung F.C.C.;
RT   "Complete genome sequence assembly of Hymenobacter sp. APR13.";
RL   Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
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};
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};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC   -!- SIMILARITY: Belongs to the FPG family. {ECO:0000256|ARBA:ARBA00009409}.
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DR   EMBL; CP006587; AII53472.1; -; Genomic_DNA.
DR   RefSeq; WP_044017362.1; NZ_CP006587.1.
DR   AlphaFoldDB; A0A076HXW7; -.
DR   STRING; 1356852.N008_15995; -.
DR   KEGG; hym:N008_15995; -.
DR   eggNOG; COG0266; Bacteria.
DR   HOGENOM; CLU_038423_0_2_10; -.
DR   OrthoDB; 9800855at2; -.
DR   Proteomes; UP000028590; Chromosome.
DR   GO; GO:0140078; F:class I DNA-(apurinic or apyrimidinic site) endonuclease activity; IEA:RHEA.
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-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006284; P:base-excision repair; IEA:InterPro.
DR   Gene3D; 1.10.8.50; -; 1.
DR   Gene3D; 3.20.190.10; MutM-like, N-terminal; 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   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   SMART; SM00898; Fapy_DNA_glyco; 1.
DR   SMART; SM01232; H2TH; 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};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028590};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00391}.
FT   DOMAIN          2..114
FT                   /note="Formamidopyrimidine-DNA glycosylase catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51068"
FT   DOMAIN          224..270
FT                   /note="FPG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51066"
SQ   SEQUENCE   276 AA;  30808 MW;  BA1A397576D81A97 CRC64;
     MPELPEVETY RRFLDDLVVD QTITALEVKD PKVLATDEDT LRRALTGRTV TRTSRLGKNC
     FLHLDDDRVL VLHFGMTGDV GAYRDEPDAP RFTRVALHLG SGLCVAFVDA RKFGRIRLAE
     GVAQYQKAKK LGPDALDITA AQLQQALGTR KPMIKPLLLD QSITAGLGNW IVDEVLFQAR
     IHPERRAHTL STAEFEALHA AIQLVLSTAI RHEATYRYFP ASFLIHAREW DDSATPGTNN
     HIYCPRHPKI EIAKSYVGGR ATYYCPRCQP PPPAAA
//
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