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AGOG_NANEQ
ID   AGOG_NANEQ              Reviewed;         216 AA.
AC   Q74MX2;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=N-glycosylase/DNA lyase {ECO:0000255|HAMAP-Rule:MF_01168};
DE   AltName: Full=8-oxoguanine DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_01168};
DE            EC=3.2.2.- {ECO:0000255|HAMAP-Rule:MF_01168};
DE   AltName: Full=AGOG {ECO:0000255|HAMAP-Rule:MF_01168};
DE   AltName: Full=DNA-(apurinic or apyrimidinic site) lyase {ECO:0000255|HAMAP-Rule:MF_01168};
DE            Short=AP lyase {ECO:0000255|HAMAP-Rule:MF_01168};
DE            EC=4.2.99.18 {ECO:0000255|HAMAP-Rule:MF_01168};
GN   OrderedLocusNames=NEQ515;
OS   Nanoarchaeum equitans (strain Kin4-M).
OC   Archaea; Nanoarchaeota; Candidatus Nanoarchaeia; Nanoarchaeales;
OC   Nanoarchaeaceae; Nanoarchaeum.
OX   NCBI_TaxID=228908;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Kin4-M;
RX   PubMed=14566062; DOI=10.1073/pnas.1735403100;
RA   Waters E., Hohn M.J., Ahel I., Graham D.E., Adams M.D., Barnstead M.,
RA   Beeson K.Y., Bibbs L., Bolanos R., Keller M., Kretz K., Lin X., Mathur E.,
RA   Ni J., Podar M., Richardson T., Sutton G.G., Simon M., Soell D.,
RA   Stetter K.O., Short J.M., Noorderwier M.;
RT   "The genome of Nanoarchaeum equitans: insights into early archaeal
RT   evolution and derived parasitism.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:12984-12988(2003).
CC   -!- FUNCTION: DNA repair enzyme that is part of the base excision repair
CC       (BER) pathway; protects from oxidative damage by removing the major
CC       product of DNA oxidation, 8-oxoguanine (GO), from single- and double-
CC       stranded DNA substrates. {ECO:0000255|HAMAP-Rule:MF_01168}.
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:0000255|HAMAP-
CC         Rule:MF_01168};
CC   -!- DOMAIN: Contains two alpha-helical subdomains, with the 8-oxoguanine
CC       binding site located in a cleft at their interface. Contains a helix-
CC       hairpin-helix (HhH) structural motif and a Gly/Pro-rich sequence
CC       followed by a conserved Asp (HhH-GPD motif).
CC   -!- SIMILARITY: Belongs to the archaeal N-glycosylase/DNA lyase (AGOG)
CC       family. {ECO:0000255|HAMAP-Rule:MF_01168}.
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DR   EMBL; AE017199; AAR39356.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q74MX2; -.
DR   SMR; Q74MX2; -.
DR   STRING; 228908.NEQ515; -.
DR   EnsemblBacteria; AAR39356; AAR39356; NEQ515.
DR   KEGG; neq:NEQ515; -.
DR   PATRIC; fig|228908.8.peg.534; -.
DR   HOGENOM; CLU_085935_0_0_2; -.
DR   OMA; VKMFGYA; -.
DR   BioCyc; NEQU228908:GJB6-547-MON; -.
DR   Proteomes; UP000000578; Chromosome.
DR   GO; GO:0140078; F:class I DNA-(apurinic or apyrimidinic site) endonuclease activity; IEA:UniProtKB-EC.
DR   GO; GO:0000702; F:oxidized base lesion DNA N-glycosylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006284; P:base-excision repair; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01168; AGOG; 1.
DR   InterPro; IPR016544; AGOG.
DR   InterPro; IPR015254; AGOG-like.
DR   InterPro; IPR011257; DNA_glycosylase.
DR   Pfam; PF09171; AGOG; 2.
DR   PIRSF; PIRSF008955; AGOG; 1.
DR   SUPFAM; SSF48150; SSF48150; 1.
PE   3: Inferred from homology;
KW   DNA damage; DNA excision; DNA repair; Hydrolase; Lyase; Reference proteome.
FT   CHAIN           1..216
FT                   /note="N-glycosylase/DNA lyase"
FT                   /id="PRO_0000185111"
FT   REGION          106..170
FT                   /note="Helix-hairpin-helix"
FT   ACT_SITE        130
FT                   /note="Schiff-base intermediate with DNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01168"
FT   ACT_SITE        162
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01168"
FT   BINDING         27
FT                   /ligand="8-oxoguanine"
FT                   /ligand_id="ChEBI:CHEBI:52617"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01168"
FT   BINDING         48
FT                   /ligand="8-oxoguanine"
FT                   /ligand_id="ChEBI:CHEBI:52617"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01168"
FT   BINDING         59
FT                   /ligand="8-oxoguanine"
FT                   /ligand_id="ChEBI:CHEBI:52617"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01168"
FT   BINDING         134
FT                   /ligand="8-oxoguanine"
FT                   /ligand_id="ChEBI:CHEBI:52617"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01168"
FT   BINDING         160
FT                   /ligand="8-oxoguanine"
FT                   /ligand_id="ChEBI:CHEBI:52617"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01168"
FT   BINDING         190
FT                   /ligand="8-oxoguanine"
FT                   /ligand_id="ChEBI:CHEBI:52617"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01168"
FT   BINDING         194
FT                   /ligand="8-oxoguanine"
FT                   /ligand_id="ChEBI:CHEBI:52617"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01168"
SQ   SEQUENCE   216 AA;  26005 MW;  DC1D0C211503B3FA CRC64;
     MEDPLIKILK QFSIEDAKYV EYNLDRQFLA LKENPKPVGL VIANALISYQ LTMPGERYWE
     LFAKKVNSFN DLYDFVKKYN PRFLSNKLKR LERFKPYIDI IEQNREHYYE NMVALNKFLA
     KIMNQNIYDK TIVFSIKMFA YAMRALGYKF KPFPFEIAIP LDYRLKKINP DLNYWFYVSK
     QTNIPPLHID SLIWPIFRIK NLPKKFALLK EYLSNL
 
 
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