OGG1_ARATH
ID OGG1_ARATH Reviewed; 365 AA.
AC Q9FNY7; Q9XI06;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=N-glycosylase/DNA lyase OGG1;
DE Includes:
DE RecName: Full=8-oxoguanine DNA glycosylase 1;
DE Short=AtOGG1;
DE EC=3.2.2.-;
DE Includes:
DE RecName: Full=DNA-(apurinic or apyrimidinic site) lyase;
DE Short=AP lyase;
DE EC=4.2.99.18 {ECO:0000269|PubMed:11361340, ECO:0000269|PubMed:11785940, ECO:0000269|PubMed:12627976};
GN Name=OGG1; OrderedLocusNames=At1g21710; ORFNames=F8K7.14;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=cv. Columbia;
RX PubMed=11361340; DOI=10.1007/s004380000414;
RA Dany A.L., Tissier A.;
RT "A functional OGG1 homologue from Arabidopsis thaliana.";
RL Mol. Genet. Genomics 265:293-301(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP SPECIFICITY.
RX PubMed=11785940; DOI=10.1023/a:1013644026132;
RA Garcia-Ortiz V., Ariza R., Roldan-Arjona T.;
RT "An OGG1 orthologue encoding a functional 8-oxoguanine DNA
RT glycosylase/lyase in Arabidopsis thaliana.";
RL Plant Mol. Biol. 47:795-804(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Kim C.J., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=12627976; DOI=10.1021/bi027226u;
RA Morales-Ruiz T., Birincioglu M., Jaruga P., Rodriguez H., Roldan-Arjona T.,
RA Dizdaroglu M.;
RT "Arabidopsis thaliana Ogg1 protein excises 8-hydroxyguanine and 2,6-
RT diamino-4-hydroxy-5-formamidopyrimidine from oxidatively damaged DNA
RT containing multiple lesions.";
RL Biochemistry 42:3089-3095(2003).
RN [8]
RP DISRUPTION PHENOTYPE.
RA Murphy T.M.;
RT "What is base excision repair good for?: knockout mutants for FPG and OGG
RT glycosylase genes in Arabidopsis.";
RL Physiol. Plantarum 123:227-233(2005).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=22473985; DOI=10.1093/jxb/ers093;
RA Chen H., Chu P., Zhou Y., Li Y., Liu J., Ding Y., Tsang E.W., Jiang L.,
RA Wu K., Huang S.;
RT "Overexpression of AtOGG1, a DNA glycosylase/AP lyase, enhances seed
RT longevity and abiotic stress tolerance in Arabidopsis.";
RL J. Exp. Bot. 63:4107-4121(2012).
CC -!- FUNCTION: Involved in repair of DNA damaged by oxidation by incising
CC DNA at 8-oxoG residues. Excises 7,8-dihydro-8-oxoguanine and 2,6-
CC diamino-4-hydroxy-5-N-methylformamidopyrimidine (Fapy) from damaged
CC DNA. Has a beta-lyase activity that nicks DNA 3' to the lesion.
CC {ECO:0000269|PubMed:11361340, ECO:0000269|PubMed:11785940,
CC ECO:0000269|PubMed:12627976, ECO:0000269|PubMed:22473985}.
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:0000269|PubMed:11361340, ECO:0000269|PubMed:11785940,
CC ECO:0000269|PubMed:12627976};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.29 uM for 8-hydroxyguanine {ECO:0000269|PubMed:12627976};
CC KM=3.6 uM for 2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine
CC (Fapy) {ECO:0000269|PubMed:12627976};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22473985}.
CC -!- TISSUE SPECIFICITY: Expressed in stems, roots, rosette and cauline
CC leaves, flowers and seeds. {ECO:0000269|PubMed:11785940,
CC ECO:0000269|PubMed:22473985}.
CC -!- DEVELOPMENTAL STAGE: Expression is induced during seed desiccation and
CC imbibition. {ECO:0000269|PubMed:22473985}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions or UV-A irradiation stress. {ECO:0000269|Ref.8}.
CC -!- MISCELLANEOUS: Transgenic seeds over-expressing OGG1 exhibit enhanced
CC seed longevity associated with reduced DNA damage, enhanced seed
CC tolerance to abiotic stresses and improved germination performance
CC under abiotic stresses. {ECO:0000305|PubMed:22473985}.
CC -!- SIMILARITY: Belongs to the type-1 OGG1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD41425.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ277400; CAC19363.1; -; mRNA.
DR EMBL; AJ302082; CAC83625.1; -; mRNA.
DR EMBL; AC007727; AAD41425.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE30145.1; -; Genomic_DNA.
DR EMBL; AK176524; BAD44287.1; -; mRNA.
DR EMBL; BT025249; ABF19002.1; -; mRNA.
DR PIR; E86350; E86350.
DR RefSeq; NP_173590.1; NM_102020.4.
DR AlphaFoldDB; Q9FNY7; -.
DR SMR; Q9FNY7; -.
DR STRING; 3702.AT1G21710.1; -.
DR PaxDb; Q9FNY7; -.
DR PRIDE; Q9FNY7; -.
DR ProteomicsDB; 250902; -.
DR EnsemblPlants; AT1G21710.1; AT1G21710.1; AT1G21710.
DR GeneID; 838775; -.
DR Gramene; AT1G21710.1; AT1G21710.1; AT1G21710.
DR KEGG; ath:AT1G21710; -.
DR Araport; AT1G21710; -.
DR TAIR; locus:2036957; AT1G21710.
DR eggNOG; KOG2875; Eukaryota.
DR HOGENOM; CLU_027543_3_1_1; -.
DR InParanoid; Q9FNY7; -.
DR OMA; YAQTYVF; -.
DR OrthoDB; 1079482at2759; -.
DR PhylomeDB; Q9FNY7; -.
DR PRO; PR:Q9FNY7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FNY7; baseline and differential.
DR Genevisible; Q9FNY7; AT.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0034039; F:8-oxo-7,8-dihydroguanine DNA N-glycosylase activity; IBA:GO_Central.
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:0008534; F:oxidized purine nucleobase lesion DNA N-glycosylase activity; IDA:TAIR.
DR GO; GO:0006285; P:base-excision repair, AP site formation; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; IDA:TAIR.
DR GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
DR CDD; cd00056; ENDO3c; 1.
DR Gene3D; 1.10.1670.10; -; 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 Pfam; PF00730; HhH-GPD; 1.
DR Pfam; PF07934; OGG_N; 1.
DR SMART; SM00478; ENDO3c; 1.
DR SUPFAM; SSF48150; SSF48150; 1.
PE 1: Evidence at protein level;
KW DNA damage; DNA repair; DNA-binding; Glycosidase; Hydrolase; Lyase;
KW Multifunctional enzyme; Nucleus; Reference proteome.
FT CHAIN 1..365
FT /note="N-glycosylase/DNA lyase OGG1"
FT /id="PRO_0000421262"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 261
FT /note="Schiff-base intermediate with DNA"
FT /evidence="ECO:0000250"
FT BINDING 162
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000250"
FT BINDING 167
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000250"
FT BINDING 215
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000250"
FT BINDING 278
FT /ligand="8-oxoguanine"
FT /ligand_id="ChEBI:CHEBI:52617"
FT /evidence="ECO:0000250"
FT BINDING 280
FT /ligand="8-oxoguanine"
FT /ligand_id="ChEBI:CHEBI:52617"
FT /evidence="ECO:0000250"
FT BINDING 282
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000250"
FT BINDING 324
FT /ligand="8-oxoguanine"
FT /ligand_id="ChEBI:CHEBI:52617"
FT /evidence="ECO:0000250"
FT BINDING 328
FT /ligand="8-oxoguanine"
FT /ligand_id="ChEBI:CHEBI:52617"
FT /evidence="ECO:0000250"
SQ SEQUENCE 365 AA; 40283 MW; 738821AD55605185 CRC64;
MKRPRPTSQP SISSTVKPPL SPPVTPILKQ KLHRTGTPKW FPLKLTHTEL TLPLTFPTGQ
TFRWKKTGAI QYSGTIGPHL VSLRQRPGDD AVSYCVHCST SPKSAELALL DFLNAEISLA
ELWSDFSKKD PRFGELARHL RGARVLRQDP LECLIQFLCS SNNNIARITK MVDFVSSLGL
HLGDIDGFEF HQFPSLDRLS RVSEEEFRKA GFGYRAKYIT GTVNALQAKP GGGNEWLLSL
RKVELQEAVA ALCTLPGVGP KVAACIALFS LDQHSAIPVD THVWQIATNY LLPDLAGAKL
TPKLHGRVAE AFVSKYGEYA GWAQTLLFIA ELPAQKTLLQ SFSQPINKLD ESAEVNETSC
DTLKP
