ID A0A2Z2LM81_9BURK Unreviewed; 271 AA. AC A0A2Z2LM81; DT 10-OCT-2018, integrated into UniProtKB/TrEMBL. DT 10-OCT-2018, sequence version 1. DT 16-JAN-2019, entry version 4. 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 RT from biofilms."; RL Int. J. Syst. Evol. Microbiol. 65:2913-2918(2015). 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:SAAS00020861}. 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}. 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 KO; K10563; -. 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 Complete proteome {ECO:0000313|Proteomes:UP000250185}; 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}; Membrane {ECO:0000256|SAM:Phobius}; 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 Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; 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 TRANSMEM 158 182 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 2 110 FPG_CAT. {ECO:0000259|PROSITE:PS51068}. FT DOMAIN 236 270 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 56 56 Proton donor; for beta-elimination FT activity. {ECO:0000256|HAMAP-Rule: FT MF_00103}. FT ACT_SITE 260 260 Proton donor; for delta-elimination FT activity. {ECO:0000256|HAMAP-Rule: FT MF_00103}. FT BINDING 89 89 DNA. {ECO:0000256|HAMAP-Rule:MF_00103}. FT BINDING 107 107 DNA. {ECO:0000256|HAMAP-Rule:MF_00103}. FT BINDING 151 151 DNA. {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 //