ID A9A4Y2_NITMS Unreviewed; 287 AA.
AC A9A4Y2;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 24-JAN-2024, entry version 74.
DE RecName: Full=DNA-(apurinic or apyrimidinic site) lyase {ECO:0000256|ARBA:ARBA00012720};
DE EC=4.2.99.18 {ECO:0000256|ARBA:ARBA00012720};
GN OrderedLocusNames=Nmar_1540 {ECO:0000313|EMBL:ABX13436.1};
OS Nitrosopumilus maritimus (strain SCM1).
OC Archaea; Nitrososphaerota; Nitrososphaeria; Nitrosopumilales;
OC Nitrosopumilaceae; Nitrosopumilus.
OX NCBI_TaxID=436308 {ECO:0000313|EMBL:ABX13436.1, ECO:0000313|Proteomes:UP000000792};
RN [1] {ECO:0000313|EMBL:ABX13436.1, ECO:0000313|Proteomes:UP000000792}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCM1 {ECO:0000313|EMBL:ABX13436.1,
RC ECO:0000313|Proteomes:UP000000792};
RX PubMed=20421470; DOI=10.1073/pnas.0913533107;
RA Walker C.B., de la Torre J.R., Klotz M.G., Urakawa H., Pinel N., Arp D.J.,
RA Brochier-Armanet C., Chain P.S., Chan P.P., Gollabgir A., Hemp J.,
RA Hugler M., Karr E.A., Konneke M., Shin M., Lawton T.J., Lowe T.,
RA Martens-Habbena W., Sayavedra-Soto L.A., Lang D., Sievert S.M.,
RA Rosenzweig A.C., Manning G., Stahl D.A.;
RT "Nitrosopumilus maritimus genome reveals unique mechanisms for
RT nitrification and autotrophy in globally distributed marine crenarchaea.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:8818-8823(2010).
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 type-1 OGG1 family.
CC {ECO:0000256|ARBA:ARBA00010679}.
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DR EMBL; CP000866; ABX13436.1; -; Genomic_DNA.
DR AlphaFoldDB; A9A4Y2; -.
DR STRING; 436308.Nmar_1540; -.
DR EnsemblBacteria; ABX13436; ABX13436; Nmar_1540.
DR KEGG; nmr:Nmar_1540; -.
DR eggNOG; arCOG00464; Archaea.
DR HOGENOM; CLU_027543_3_0_2; -.
DR InParanoid; A9A4Y2; -.
DR OMA; GYAQQYL; -.
DR OrthoDB; 14922at2157; -.
DR PhylomeDB; A9A4Y2; -.
DR Proteomes; UP000000792; Chromosome.
DR GO; GO:0034039; F:8-oxo-7,8-dihydroguanine DNA N-glycosylase activity; IBA:GO_Central.
DR GO; GO:0006285; P:base-excision repair, AP site formation; IBA:GO_Central.
DR CDD; cd00056; ENDO3c; 1.
DR Gene3D; 3.30.310.260; -; 1.
DR Gene3D; 1.10.1670.10; Helix-hairpin-Helix base-excision DNA repair enzymes (C-terminal); 1.
DR InterPro; IPR011257; DNA_glycosylase.
DR InterPro; IPR003265; HhH-GPD_domain.
DR InterPro; IPR023170; HhH_base_excis_C.
DR InterPro; IPR012904; OGG_N.
DR PANTHER; PTHR10242; 8-OXOGUANINE DNA GLYCOSYLASE; 1.
DR PANTHER; PTHR10242:SF2; N-GLYCOSYLASE/DNA LYASE; 1.
DR Pfam; PF00730; HhH-GPD; 1.
DR Pfam; PF07934; OGG_N; 1.
DR SMART; SM00478; ENDO3c; 1.
DR SUPFAM; SSF48150; DNA-glycosylase; 1.
DR SUPFAM; SSF55945; TATA-box binding protein-like; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Reference proteome {ECO:0000313|Proteomes:UP000000792}.
FT DOMAIN 108..272
FT /note="HhH-GPD"
FT /evidence="ECO:0000259|SMART:SM00478"
SQ SEQUENCE 287 AA; 33909 MW; 9C97E5B92825FF21 CRC64;
MKRFQSKMQI KQPIDVENSI NSGQVFLWRK NKEFWYGVNG QDILEVNKNG KIKSLQNYKT
DFFRNNDNFD EIIKSISKDK IVKNAVKKYP GLRIIKQDPF QCLISFIVSS NSNIQKIKTN
LENISQKFGE RVEYKDQEFF LFPNAKTLSK ASITEIKNCG VGYRAKFIKE ASKIFASEKI
MIDDLKSSDY FDAKKKIRII PGIGNKVADC ILLFSLDKLE SFPLDRWMIR ILEKYYSKKF
QIDTKTITEK QYDILHEKIV DYFGLYAGYA QQFLFKMERE NYQKKWL
//