FPG_ARATH
ID FPG_ARATH Reviewed; 390 AA.
AC O80358; O80359; Q9SBB4;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Formamidopyrimidine-DNA glycosylase;
DE Short=Fapy-DNA glycosylase;
DE EC=3.2.2.23;
DE EC=4.2.99.18;
DE AltName: Full=DNA-(apurinic or apyrimidinic site) lyase FPG1;
DE AltName: Full=Formamidopyrimidine-DNA glycosylase 1;
DE Short=AtFPG-1;
DE AltName: Full=Formamidopyrimidine-DNA glycosylase 2;
DE Short=AtFPG-2;
DE AltName: Full=Protein MutM homolog 1;
DE Short=AtMMH-1;
DE AltName: Full=Protein MutM homolog 2;
DE Short=AtMMH-2;
GN Name=FPG1; Synonyms=FPG2; OrderedLocusNames=At1g52500; ORFNames=F6D8.28;
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 [GENOMIC DNA], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=9819050; DOI=10.1007/s004380050851;
RA Ohtsubo T., Matsuda O., Iba K., Terashima I., Sekiguchi M., Nakabeppu Y.;
RT "Molecular cloning of AtMMH, an Arabidopsis thaliana ortholog of the
RT Escherichia coli mutM gene, and analysis of functional domains of its
RT product.";
RL Mol. Gen. Genet. 259:577-590(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=cv. Landsberg erecta;
RX PubMed=11535407; DOI=10.1016/s1011-1344(01)00172-5;
RA Murphy T.M., Gao M.J.;
RT "Multiple forms of formamidopyrimidine-DNA glycosylase produced by
RT alternative splicing in Arabidopsis thaliana.";
RL J. Photochem. Photobiol. B 61:87-93(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND FUNCTION.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=11272725; DOI=10.1562/0031-8655(2001)073<0128:afofdg>2.0.co;2;
RA Gao M.J., Murphy T.M.;
RT "Alternative forms of formamidopyrimidine-DNA glycosylase from Arabidopsis
RT thaliana.";
RL Photochem. Photobiol. 73:128-134(2001).
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA De Los Reyes C., Quan R., Chen H., Bautista V., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
RN [7]
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 1-304 IN COMPLEX WITH DNA,
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RX PubMed=22789755; DOI=10.1016/j.dnarep.2012.06.004;
RA Duclos S., Aller P., Jaruga P., Dizdaroglu M., Wallace S.S., Doublie S.;
RT "Structural and biochemical studies of a plant formamidopyrimidine-DNA
RT glycosylase reveal why eukaryotic Fpg glycosylases do not excise 8-
RT oxoguanine.";
RL DNA Repair 11:714-725(2012).
CC -!- FUNCTION: Involved in base excision repair of DNA damaged by oxidation
CC or by mutagenic agents. Acts as DNA glycosylase that recognizes and
CC removes damaged bases. Can process efficiently 4,6-diamino-5-
CC formamidopyrimidine (FapyA), 2,6-diamino-4- hydroxy-5-
CC formamidopyrimidine (FapyG) and the further oxidation products of 8-
CC oxoguanine (8-oxoG), such as guanidinohydantoin and
CC spiroiminodihydantoin. Has marginal activity towards 8-oxoG. Has AP
CC (apurinic/apyrimidinic) lyase activity. Cleaves the DNA backbone by
CC beta-delta elimination to generate a single-strand break at the site of
CC the removed base with both 3'- and 5'-phosphates.
CC {ECO:0000269|PubMed:11272725, ECO:0000269|PubMed:22789755,
CC ECO:0000269|PubMed:9819050}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of DNA containing ring-opened 7-methylguanine
CC residues, releasing 2,6-diamino-4-hydroxy-5-(N-
CC methyl)formamidopyrimidine.; EC=3.2.2.23;
CC Evidence={ECO:0000269|PubMed:22789755};
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|PROSITE-
CC ProRule:PRU00392, ECO:0000269|PubMed:22789755};
CC -!- SUBUNIT: Monomer. {ECO:0000305|PubMed:22789755}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O80358-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O80358-2; Sequence=VSP_045377, VSP_045378;
CC -!- TISSUE SPECIFICITY: Expressed in leaves (at protein levels).
CC {ECO:0000269|PubMed:9819050}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions or UV-A irradiation stress. {ECO:0000269|Ref.7}.
CC -!- SIMILARITY: Belongs to the FPG family. {ECO:0000255|PROSITE-
CC ProRule:PRU00392}.
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DR EMBL; AB010690; BAA32702.1; -; Genomic_DNA.
DR EMBL; AB010690; BAA32703.1; -; Genomic_DNA.
DR EMBL; AF099970; AAC97952.1; -; mRNA.
DR EMBL; AF099971; AAC97953.1; -; mRNA.
DR EMBL; AC008016; AAD55612.1; -; Genomic_DNA.
DR EMBL; AC008016; AAD55613.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32814.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32815.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60729.1; -; Genomic_DNA.
DR EMBL; BT043496; ACG58696.1; -; mRNA.
DR PIR; E96565; E96565.
DR PIR; T51713; T51713.
DR PIR; T51714; T51714.
DR RefSeq; NP_001322993.1; NM_001333547.1. [O80358-2]
DR RefSeq; NP_564608.1; NM_104128.3. [O80358-1]
DR RefSeq; NP_849798.1; NM_179467.3. [O80358-2]
DR PDB; 3TWK; X-ray; 2.30 A; A/B=1-281.
DR PDB; 3TWL; X-ray; 1.70 A; A=1-304.
DR PDB; 3TWM; X-ray; 2.80 A; A/B=1-304.
DR PDBsum; 3TWK; -.
DR PDBsum; 3TWL; -.
DR PDBsum; 3TWM; -.
DR AlphaFoldDB; O80358; -.
DR SMR; O80358; -.
DR STRING; 3702.AT1G52500.2; -.
DR iPTMnet; O80358; -.
DR PaxDb; O80358; -.
DR PRIDE; O80358; -.
DR ProteomicsDB; 229997; -. [O80358-1]
DR EnsemblPlants; AT1G52500.1; AT1G52500.1; AT1G52500. [O80358-2]
DR EnsemblPlants; AT1G52500.2; AT1G52500.2; AT1G52500. [O80358-1]
DR EnsemblPlants; AT1G52500.3; AT1G52500.3; AT1G52500. [O80358-2]
DR GeneID; 841681; -.
DR Gramene; AT1G52500.1; AT1G52500.1; AT1G52500. [O80358-2]
DR Gramene; AT1G52500.2; AT1G52500.2; AT1G52500. [O80358-1]
DR Gramene; AT1G52500.3; AT1G52500.3; AT1G52500. [O80358-2]
DR KEGG; ath:AT1G52500; -.
DR Araport; AT1G52500; -.
DR TAIR; locus:2035195; AT1G52500.
DR eggNOG; ENOG502QVDB; Eukaryota.
DR HOGENOM; CLU_038423_0_0_1; -.
DR InParanoid; O80358; -.
DR OMA; LQYCPTC; -.
DR OrthoDB; 1467835at2759; -.
DR PhylomeDB; O80358; -.
DR BRENDA; 3.2.2.23; 399.
DR PRO; PR:O80358; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O80358; baseline and differential.
DR Genevisible; O80358; AT.
DR GO; GO:0005634; C:nucleus; 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:0019104; F:DNA N-glycosylase activity; IDA:TAIR.
DR GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) endonuclease activity; IBA:GO_Central.
DR GO; GO:0008534; F:oxidized purine nucleobase lesion DNA N-glycosylase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006284; P:base-excision repair; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; IDA:TAIR.
DR GO; GO:0006979; P:response to oxidative stress; TAS:TAIR.
DR Gene3D; 3.20.190.10; -; 1.
DR InterPro; IPR015886; DNA_glyclase/AP_lyase_DNA-bd.
DR InterPro; IPR020629; Formamido-pyr_DNA_Glyclase.
DR InterPro; IPR012319; FPG_cat.
DR InterPro; IPR035937; MutM-like_N-ter.
DR InterPro; IPR010979; Ribosomal_S13-like_H2TH.
DR Pfam; PF01149; Fapy_DNA_glyco; 1.
DR Pfam; PF06831; H2TH; 1.
DR SMART; SM00898; Fapy_DNA_glyco; 1.
DR SMART; SM01232; H2TH; 1.
DR SUPFAM; SSF46946; SSF46946; 1.
DR SUPFAM; SSF81624; SSF81624; 1.
DR TIGRFAMs; TIGR00577; fpg; 1.
DR PROSITE; PS51068; FPG_CAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; DNA damage; DNA repair; DNA-binding;
KW Glycosidase; Hydrolase; Lyase; Multifunctional enzyme; Nucleus;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..390
FT /note="Formamidopyrimidine-DNA glycosylase"
FT /id="PRO_0000421261"
FT REGION 283..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..301
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..382
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 2
FT /note="Schiff-base intermediate with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00392"
FT ACT_SITE 3
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00392"
FT ACT_SITE 60
FT /note="Proton donor; for beta-elimination activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00392"
FT BINDING 107
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000269|PubMed:22789755"
FT BINDING 126
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:0000269|PubMed:22789755"
FT BINDING 186
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000269|PubMed:22789755"
FT VAR_SEQ 224..274
FT /note="EKAVEVDADSSQFPSYWIFHNREKKPGKAFVDGKKIDFITAGGRTTAYVPE
FT -> QHAVQVNADSKEFPVEWLFHFRWGKKAGKVNGKLSHHLSINLMKQNLGFCR (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:11272725"
FT /id="VSP_045377"
FT VAR_SEQ 275..390
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11272725"
FT /id="VSP_045378"
FT CONFLICT 239
FT /note="Y -> N (in Ref. 2; AAC97952)"
FT /evidence="ECO:0000305"
FT HELIX 4..17
FT /evidence="ECO:0007829|PDB:3TWL"
FT TURN 18..20
FT /evidence="ECO:0007829|PDB:3TWM"
FT STRAND 22..28
FT /evidence="ECO:0007829|PDB:3TWL"
FT TURN 32..34
FT /evidence="ECO:0007829|PDB:3TWL"
FT HELIX 40..47
FT /evidence="ECO:0007829|PDB:3TWL"
FT STRAND 51..58
FT /evidence="ECO:0007829|PDB:3TWL"
FT STRAND 61..69
FT /evidence="ECO:0007829|PDB:3TWL"
FT STRAND 71..75
FT /evidence="ECO:0007829|PDB:3TWL"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:3TWL"
FT STRAND 81..85
FT /evidence="ECO:0007829|PDB:3TWL"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:3TWK"
FT STRAND 108..114
FT /evidence="ECO:0007829|PDB:3TWL"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:3TWK"
FT STRAND 119..123
FT /evidence="ECO:0007829|PDB:3TWL"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:3TWL"
FT STRAND 130..135
FT /evidence="ECO:0007829|PDB:3TWL"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:3TWL"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:3TWL"
FT TURN 150..152
FT /evidence="ECO:0007829|PDB:3TWL"
FT HELIX 157..165
FT /evidence="ECO:0007829|PDB:3TWL"
FT HELIX 171..176
FT /evidence="ECO:0007829|PDB:3TWL"
FT TURN 178..180
FT /evidence="ECO:0007829|PDB:3TWL"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:3TWL"
FT HELIX 186..195
FT /evidence="ECO:0007829|PDB:3TWL"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:3TWL"
FT HELIX 209..228
FT /evidence="ECO:0007829|PDB:3TWL"
FT TURN 229..231
FT /evidence="ECO:0007829|PDB:3TWL"
FT HELIX 233..235
FT /evidence="ECO:0007829|PDB:3TWL"
FT HELIX 241..244
FT /evidence="ECO:0007829|PDB:3TWL"
FT STRAND 260..264
FT /evidence="ECO:0007829|PDB:3TWK"
FT STRAND 267..271
FT /evidence="ECO:0007829|PDB:3TWK"
FT TURN 273..275
FT /evidence="ECO:0007829|PDB:3TWL"
FT HELIX 280..286
FT /evidence="ECO:0007829|PDB:3TWL"
SQ SEQUENCE 390 AA; 43194 MW; F6B5E0DAFD6FD010 CRC64;
MPELPEVEAA RRAIEENCLG KKIKRVIIAD DNKVIHGISP SDFQTSILGK TIISARRKGK
NLWLELDSPP FPSFQFGMAG AIYIKGVAVT KYKRSAVKDS EEWPSKYSKF FVELDDGLEL
SFTDKRRFAK VRLLANPTSV SPISELGPDA LLEPMTVDEF AESLAKKKIT IKPLLLDQGY
ISGIGNWIAD EVLYQARIHP LQTASSLSKE QCEALHTSIK EVIEKAVEVD ADSSQFPSYW
IFHNREKKPG KAFVDGKKID FITAGGRTTA YVPELQKLYG KDAEKAAKVR PAKRGVKPKE
DDGDGEEDEQ ETEKEDESAK SKKGQKPRGG RGKKPASKTK TEESDDDGDD SEAEEEVVKP
KGRGTKPAIK RKSEEKATSQ AGKKPKGRKS
