ID A0A073CFV4_PLAAG Unreviewed; 239 AA.
AC A0A073CFV4;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Endonuclease III {ECO:0000256|HAMAP-Rule:MF_00942};
DE EC=4.2.99.18 {ECO:0000256|HAMAP-Rule:MF_00942};
DE AltName: Full=DNA-(apurinic or apyrimidinic site) lyase {ECO:0000256|HAMAP-Rule:MF_00942};
GN Name=nth {ECO:0000256|HAMAP-Rule:MF_00942,
GN ECO:0000313|EMBL:KEI67011.1};
GN ORFNames=A19Y_2042 {ECO:0000313|EMBL:KEI67011.1};
OS Planktothrix agardhii NIVA-CYA 126/8.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Microcoleaceae; Planktothrix.
OX NCBI_TaxID=388467 {ECO:0000313|EMBL:KEI67011.1, ECO:0000313|Proteomes:UP000027395};
RN [1] {ECO:0000313|EMBL:KEI67011.1, ECO:0000313|Proteomes:UP000027395}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIVA-CYA 126/8 {ECO:0000313|EMBL:KEI67011.1,
RC ECO:0000313|Proteomes:UP000027395};
RX PubMed=24907328; DOI=10.1128/AEM.01188-14;
RA Christiansen G., Goesmann A., Kurmayer R.;
RT "Elucidation of insertion elements encoded on plasmids and in vitro
RT construction of shuttle vectors from the toxic cyanobacterium
RT Planktothrix.";
RL Appl. Environ. Microbiol. 80:4887-4897(2014).
CC -!- FUNCTION: DNA repair enzyme that has both DNA N-glycosylase activity
CC and AP-lyase activity. The DNA N-glycosylase activity releases various
CC damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving
CC an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the
CC phosphodiester bond 3' to the AP site by a beta-elimination, leaving a
CC 3'-terminal unsaturated sugar and a product with a terminal 5'-
CC phosphate. {ECO:0000256|HAMAP-Rule:MF_00942}.
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; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_00942};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00942};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000256|HAMAP-Rule:MF_00942};
CC -!- SIMILARITY: Belongs to the Nth/MutY family.
CC {ECO:0000256|ARBA:ARBA00008343, ECO:0000256|HAMAP-Rule:MF_00942}.
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DR EMBL; CM002803; KEI67011.1; -; Genomic_DNA.
DR RefSeq; WP_042153981.1; NZ_CM002803.1.
DR AlphaFoldDB; A0A073CFV4; -.
DR STRING; 388467.A19Y_2042; -.
DR GeneID; 77289437; -.
DR PATRIC; fig|388467.6.peg.1990; -.
DR eggNOG; COG0177; Bacteria.
DR HOGENOM; CLU_012862_3_3_3; -.
DR Proteomes; UP000027395; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0140078; F:class I DNA-(apurinic or apyrimidinic site) endonuclease activity; IEA:UniProtKB-EC.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019104; F:DNA N-glycosylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006284; P:base-excision repair; IEA:InterPro.
DR CDD; cd00056; ENDO3c; 1.
DR Gene3D; 1.10.1670.10; Helix-hairpin-Helix base-excision DNA repair enzymes (C-terminal); 1.
DR HAMAP; MF_00942; Nth; 1.
DR InterPro; IPR011257; DNA_glycosylase.
DR InterPro; IPR003651; Endonuclease3_FeS-loop_motif.
DR InterPro; IPR003265; HhH-GPD_domain.
DR InterPro; IPR023170; HhH_base_excis_C.
DR InterPro; IPR005759; Nth.
DR NCBIfam; TIGR01083; nth; 1.
DR PANTHER; PTHR10359; A/G-SPECIFIC ADENINE GLYCOSYLASE/ENDONUCLEASE III; 1.
DR PANTHER; PTHR10359:SF18; ENDONUCLEASE III; 1.
DR Pfam; PF00730; HhH-GPD; 1.
DR PIRSF; PIRSF001435; Nth; 1.
DR SMART; SM00478; ENDO3c; 1.
DR SMART; SM00525; FES; 1.
DR SUPFAM; SSF48150; DNA-glycosylase; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_00942};
KW DNA damage {ECO:0000256|HAMAP-Rule:MF_00942};
KW DNA repair {ECO:0000256|HAMAP-Rule:MF_00942};
KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_00942};
KW Glycosidase {ECO:0000256|HAMAP-Rule:MF_00942};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00942};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_00942};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW Rule:MF_00942};
KW Lyase {ECO:0000256|HAMAP-Rule:MF_00942, ECO:0000313|EMBL:KEI67011.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00942}; Reference proteome {ECO:0000313|Proteomes:UP000027395}.
FT DOMAIN 45..193
FT /note="HhH-GPD"
FT /evidence="ECO:0000259|SMART:SM00478"
FT BINDING 195
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00942"
FT BINDING 202
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00942"
FT BINDING 205
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00942"
FT BINDING 211
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00942"
SQ SEQUENCE 239 AA; 26744 MW; 7D1D2F4774A1D52F CRC64;
MVTQKKRNPK QRALEILLRL KRLYPDATCS LNYQTPVQLL VATILSAQCT DERVNQVTPA
LFARFPDAQS LAKADITELE TLVRSTGFYR NKARHIQGSC QLLAEKYGGQ PPKVMEQLLE
LPGVARKTAN VVLAHGYGIN MGVTVDTHVK RLSQRLGLTS HNDPIRIERD LMPLIPREDW
ENWSIRLIYH GRAVCTARSP MCYNCELSDL CPSAQGSTVP SAGKKLGFSI NNYLQGEQP
//
