ID A0A1X1RRD4_MYCCE Unreviewed; 264 AA.
AC A0A1X1RRD4;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 31.
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=AWB95_10120 {ECO:0000313|EMBL:ORV13941.1}, CQY23_04075
GN {ECO:0000313|EMBL:PIB80212.1};
OS Mycobacterium celatum.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=28045 {ECO:0000313|EMBL:ORV13941.1, ECO:0000313|Proteomes:UP000193907};
RN [1] {ECO:0000313|EMBL:ORV13941.1, ECO:0000313|Proteomes:UP000193907}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44243 {ECO:0000313|EMBL:ORV13941.1,
RC ECO:0000313|Proteomes:UP000193907};
RA Tarcisio F., Conor M., Antonella G., Elisabetta G., Giulia F.S., Sara T.,
RA Anna F., Clotilde B., Roberto B., Veronica D.S., Fabio R., Monica P.,
RA Olivier J., Enrico T., Nicola S.;
RT "The new phylogeny of the genus Mycobacterium.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PIB80212.1, ECO:0000313|Proteomes:UP000230971}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 12882 {ECO:0000313|EMBL:PIB80212.1,
RC ECO:0000313|Proteomes:UP000230971};
RX PubMed=29030295; DOI=10.1016/j.meegid.2017.10.013;
RA Tortoli E., Fedrizzi T., Meehan C.J., Trovato A., Grottola A.,
RA Giacobazzi E., Serpini G.F., Tagliazucchi S., Fabio A., Bettua C.,
RA Bertorelli R., Frascaro F., De Sanctis V., Pecorari M., Jousson O.,
RA Segata N., Cirillo D.M.;
RT "The new phylogeny of the genus Mycobacterium: The old and the news.";
RL Infect. Genet. Evol. 56:19-25(2017).
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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:ORV13941.1}.
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DR EMBL; LQOM01000025; ORV13941.1; -; Genomic_DNA.
DR EMBL; PDKV01000003; PIB80212.1; -; Genomic_DNA.
DR RefSeq; WP_062538956.1; NZ_PDKV01000003.1.
DR STRING; 28045.AWB95_10120; -.
DR OrthoDB; 9800855at2; -.
DR Proteomes; UP000193907; Unassembled WGS sequence.
DR Proteomes; UP000230971; 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 InterPro; IPR010663; Znf_FPG/IleRS.
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 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; 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 Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00391}.
FT DOMAIN 230..264
FT /note="FPG-type"
FT /evidence="ECO:0000259|PROSITE:PS51066"
SQ SEQUENCE 264 AA; 29362 MW; 621329D40AC61C59 CRC64;
MPEGHTLHRL ARLHQRRFAG APVAVSSPQG RFAAAAAAVD GRVLRRTSVW GKHLFHHYAD
GPIVHVHLGL YGTFTEHATP MPAPAGQVRM RMVGAEYGTD LRGPTVCELL DDAQVADVVA
RLGPDPLRRD ADPQWAWARI TKSRRPIGAL LMDQTVIAGV GNVYRSELLF RHAIDPYRLG
RAITEAEFTA AWTDLVALMK VGLRRGKIIV VRPEHDHGAP SYLPDRPRTY VYRRAGDPCR
VCGTTVRTAE LEGRNVFWCP ECQR
//
