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Database: UniProt
Entry: A0A1Q5DXG3_9ACTN
LinkDB: A0A1Q5DXG3_9ACTN
Original site: A0A1Q5DXG3_9ACTN 
ID   A0A1Q5DXG3_9ACTN        Unreviewed;       269 AA.
AC   A0A1Q5DXG3;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=DNA-(apurinic or apyrimidinic site) lyase {ECO:0000256|ARBA:ARBA00012720};
DE            EC=4.2.99.18 {ECO:0000256|ARBA:ARBA00012720};
GN   ORFNames=AMK18_17645 {ECO:0000313|EMBL:OKJ00468.1};
OS   Streptomyces sp. CB01249.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1703929 {ECO:0000313|EMBL:OKJ00468.1, ECO:0000313|Proteomes:UP000186839};
RN   [1] {ECO:0000313|EMBL:OKJ00468.1, ECO:0000313|Proteomes:UP000186839}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CB01249 {ECO:0000313|EMBL:OKJ00468.1,
RC   ECO:0000313|Proteomes:UP000186839};
RX   PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA   Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA   Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA   Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT   "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL   MBio 7:e02104-e02116(2016).
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   -!- SIMILARITY: Belongs to the FPG family. {ECO:0000256|ARBA:ARBA00009409}.
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:OKJ00468.1}.
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DR   EMBL; LISW01000003; OKJ00468.1; -; Genomic_DNA.
DR   RefSeq; WP_073863525.1; NZ_LISW01000003.1.
DR   AlphaFoldDB; A0A1Q5DXG3; -.
DR   OrthoDB; 9800855at2; -.
DR   Proteomes; UP000186839; 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:0019104; F:DNA N-glycosylase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006284; P:base-excision repair; IEA:InterPro.
DR   CDD; cd08970; AcNei1_N; 1.
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; IPR015887; DNA_glyclase_Znf_dom_DNA_BS.
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   PANTHER; PTHR42697; ENDONUCLEASE 8; 1.
DR   PANTHER; PTHR42697:SF3; ENDONUCLEASE 8 1; 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; 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};
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:UP000186839};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00391}.
FT   DOMAIN          2..99
FT                   /note="Formamidopyrimidine-DNA glycosylase catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51068"
FT   DOMAIN          234..268
FT                   /note="FPG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51066"
SQ   SEQUENCE   269 AA;  30109 MW;  3298E5392B129082 CRC64;
     MPEGHTIHRL AADHRERFAG RPVRTSSPQG KFSDSAALLD GHVLDTADAH GKHLFLGFGD
     TGWVHIHLGL FGKLNFGTVP APPPTDTVRL RLVNDAHHAD LRGPTTCALI TDAEKRAIHD
     RLGPDPLRED EDGERAWQRI SRSRITVAAL LMDQKVIAGV GNVYRAEVLF RHGIDPYRAG
     KDLTRREWDA IWADLRELMR EGVRNNRIDT VRPEHLPEAM GRPPRVDDHG GEVYVYRRAR
     QGCHICGTEI RTADLAARNL FWCPGCQSA
//
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