ID A0A2Z2LM81_9BURK Unreviewed; 271 AA. AC A0A2Z2LM81; DT 10-OCT-2018, integrated into UniProtKB/TrEMBL. DT 10-OCT-2018, sequence version 1. DT 02-DEC-2020, entry version 7. 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=BA022_10590 {ECO:0000313|EMBL:ASI68945.1}; OS Diaphorobacter polyhydroxybutyrativorans. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Diaphorobacter. OX NCBI_TaxID=1546149 {ECO:0000313|EMBL:ASI68945.1, ECO:0000313|Proteomes:UP000250185}; RN [1] {ECO:0000313|EMBL:ASI68945.1, ECO:0000313|Proteomes:UP000250185} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SL-205 {ECO:0000313|EMBL:ASI68945.1, RC ECO:0000313|Proteomes:UP000250185}; RX PubMed=26012582; DOI=10.1099/ijs.0.000353; RA Qiu T., Zuo Z., Gao J., Gao M., Han M., Sun L., Zhang L., Wang X.; RT "Diaphorobacter polyhydroxybutyrativorans sp. nov., a novel poly(3- RT hydroxybutyrate-co-3-hydroxyvalerate)-degrading bacterium isolated from RT biofilms."; RL Int. J. Syst. Evol. Microbiol. 65:2913-2918(2015). 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=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 -!- CATALYTIC ACTIVITY: CC Reaction=The C-O-P bond 3' to the apurinic or apyrimidinic site in DNA CC is broken by a beta-elimination reaction, leaving a 3'-terminal CC unsaturated sugar and a product with a terminal 5'-phosphate.; CC EC=4.2.99.18; Evidence={ECO:0000256|ARBA:ARBA00000643, CC ECO:0000256|HAMAP-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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP016278; ASI68945.1; -; Genomic_DNA. DR KEGG; dpy:BA022_10590; -. DR Proteomes; UP000250185; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. 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; 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_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; 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 Membrane {ECO:0000256|SAM:Phobius}; 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}; Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; 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, ECO:0000256|PROSITE-ProRule:PRU00391}. FT TRANSMEM 158..182 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 2..110 FT /note="FPG_CAT" 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 56 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 89 FT /note="DNA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00103" FT BINDING 107 FT /note="DNA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00103" FT BINDING 151 FT /note="DNA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00103" SQ SEQUENCE 271 AA; 29557 MW; 8636C032E19B787E CRC64; MPELPEVEVT RRSFAGAIEG ATVCGIAVGK PLRWPLGMEP AVLVGRRVCG VRRRGKYLLL DLDEGLLLIH LGMSGSLRFA RDLPARGAHD HFELITDHGT LRLHDPRRFG AVVWAAGESD PRARKLLDGW GLEPLGEDFA FESFHAGLRA KRTPIKQLLL AGTVVVGVGN IYACEVLFLA GIRPTTRACA IGPQRARRLH GAIREVLARA VERGGSTLRD FSSADGSAGH FQLEANVYGR AGLPCRQCGT PVRLLRQGQR STYFCPHCQR A //