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AGOG_AERPE
ID   AGOG_AERPE              Reviewed;         288 AA.
AC   Q9YE60;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 2.
DT   03-AUG-2022, entry version 89.
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=APE_0710.1;
OS   Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS   K1).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Aeropyrum.
OX   NCBI_TaxID=272557;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX   PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA   Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA   Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA   Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA   Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT   "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT   Aeropyrum pernix K1.";
RL   DNA Res. 6:83-101(1999).
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; BA000002; BAA79686.2; -; Genomic_DNA.
DR   PIR; F72660; F72660.
DR   AlphaFoldDB; Q9YE60; -.
DR   SMR; Q9YE60; -.
DR   STRING; 272557.APE_0710.1; -.
DR   EnsemblBacteria; BAA79686; BAA79686; APE_0710.1.
DR   KEGG; ape:APE_0710.1; -.
DR   eggNOG; arCOG04144; Archaea.
DR   Proteomes; UP000002518; 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   Gene3D; 1.10.1670.10; -; 1.
DR   HAMAP; MF_01168; AGOG; 1.
DR   InterPro; IPR016544; AGOG.
DR   InterPro; IPR015254; AGOG-like.
DR   InterPro; IPR011257; DNA_glycosylase.
DR   InterPro; IPR023170; HhH_base_excis_C.
DR   Pfam; PF09171; AGOG; 1.
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..288
FT                   /note="N-glycosylase/DNA lyase"
FT                   /id="PRO_0000185108"
FT   REGION          134..203
FT                   /note="Helix-hairpin-helix"
FT   ACT_SITE        160
FT                   /note="Schiff-base intermediate with DNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01168"
FT   ACT_SITE        191
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01168"
FT   BINDING         35
FT                   /ligand="8-oxoguanine"
FT                   /ligand_id="ChEBI:CHEBI:52617"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01168"
FT   BINDING         62
FT                   /ligand="8-oxoguanine"
FT                   /ligand_id="ChEBI:CHEBI:52617"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01168"
FT   BINDING         73
FT                   /ligand="8-oxoguanine"
FT                   /ligand_id="ChEBI:CHEBI:52617"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01168"
FT   BINDING         164
FT                   /ligand="8-oxoguanine"
FT                   /ligand_id="ChEBI:CHEBI:52617"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01168"
FT   BINDING         189
FT                   /ligand="8-oxoguanine"
FT                   /ligand_id="ChEBI:CHEBI:52617"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01168"
FT   BINDING         238
FT                   /ligand="8-oxoguanine"
FT                   /ligand_id="ChEBI:CHEBI:52617"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01168"
FT   BINDING         242
FT                   /ligand="8-oxoguanine"
FT                   /ligand_id="ChEBI:CHEBI:52617"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01168"
SQ   SEQUENCE   288 AA;  31443 MW;  A57E5A1F0A2786C3 CRC64;
     MAQRVRWERV ERVAEAFSRL SIGEVLGFEE QVDPQYKLVS RLAGEIGAGK AALSALLVGL
     ASYRLAMRGE EWWLCFYRHM RSSLPRAEGL RGVLRAVEGF LTSCSGAAIG REAKLRRVRR
     AASAAEVLGE VLDNPLVLVE RPSEVLEALR VALGEKGFRK TTVFSVKIAY YAVRPLAGRK
     PLTLDVPIPV DVRVACASIS SEMVEAPSYR EVVARPEAAQ RAWGRVARSS GIPVLHIDSI
     LWVTGWAPRE LPPGEAREAV AGILSRALDR GKAVLLASEL VRRPCPGG
 
 
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