NTH1_YEAST
ID NTH1_YEAST Reviewed; 399 AA.
AC P31378; D6VPK3;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Endonuclease III homolog 1 {ECO:0000255|HAMAP-Rule:MF_03183};
DE EC=3.2.2.- {ECO:0000255|HAMAP-Rule:MF_03183};
DE EC=4.2.99.18 {ECO:0000255|HAMAP-Rule:MF_03183, ECO:0000269|PubMed:14500818, ECO:0000269|PubMed:20194111, ECO:0000269|PubMed:9545197};
DE AltName: Full=Bifunctional DNA N-glycosylase/DNA-(apurinic or apyrimidinic site) lyase 1 {ECO:0000255|HAMAP-Rule:MF_03183};
DE Short=DNA glycosylase/AP lyase 1 {ECO:0000255|HAMAP-Rule:MF_03183};
DE AltName: Full=Endonuclease III-like glycosylase 1;
DE AltName: Full=Redoxyendonuclease 1;
DE Flags: Precursor;
GN Name=NTG1 {ECO:0000255|HAMAP-Rule:MF_03183}; Synonyms=OGG2, SCR1;
GN OrderedLocusNames=YAL015C; ORFNames=FUN33;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204511 / S288c / AB972;
RX PubMed=8458570; DOI=10.1139/g93-005;
RA Ouellette B.F.F., Clark M.W., Keng T., Storms R.K., Zhong W.-W., Zeng B.,
RA Fortin N., Delaney S., Barton A.B., Kaback D.B., Bussey H.;
RT "Sequencing of chromosome I from Saccharomyces cerevisiae: analysis of a 32
RT kb region between the LTE1 and SPO7 genes.";
RL Genome 36:32-42(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204511 / S288c / AB972;
RX PubMed=8144453; DOI=10.1128/jb.176.7.1872-1880.1994;
RA Barton A.B., Kaback D.B.;
RT "Molecular cloning of chromosome I DNA from Saccharomyces cerevisiae:
RT analysis of the genes in the FUN38-MAK16-SPO7 region.";
RL J. Bacteriol. 176:1872-1880(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7731988; DOI=10.1073/pnas.92.9.3809;
RA Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N.,
RA Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J.,
RA Storms R.K.;
RT "The nucleotide sequence of chromosome I from Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP FUNCTION.
RX PubMed=8805338; DOI=10.1016/s0960-9822(02)00641-3;
RA Nash H.M., Bruner S.D., Scharer O.D., Kawate T., Addona T.A., Spooner E.,
RA Lane W.S., Verdine G.L.;
RT "Cloning of a yeast 8-oxoguanine DNA glycosylase reveals the existence of a
RT base-excision DNA-repair protein superfamily.";
RL Curr. Biol. 6:968-980(1996).
RN [6]
RP FUNCTION, AND INDUCTION BY DNA DAMAGE.
RX PubMed=8855249; DOI=10.1073/pnas.93.20.10735;
RA Eide L., Bjoras M., Pirovano M., Alseth I., Berdal K.G., Seeberg E.;
RT "Base excision of oxidative purine and pyrimidine DNA damage in
RT Saccharomyces cerevisiae by a DNA glycosylase with sequence similarity to
RT endonuclease III from Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:10735-10740(1996).
RN [7]
RP FUNCTION.
RX PubMed=9020769; DOI=10.1021/bi9625511;
RA Augeri L., Lee Y.M., Barton A.B., Doetsch P.W.;
RT "Purification, characterization, gene cloning, and expression of
RT Saccharomyces cerevisiae redoxyendonuclease, a homolog of Escherichia coli
RT endonuclease III.";
RL Biochemistry 36:721-729(1997).
RN [8]
RP FUNCTION, SUBSTRATES, INDUCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=9558341; DOI=10.1021/bi973042h;
RA You H.J., Swanson R.L., Doetsch P.W.;
RT "Saccharomyces cerevisiae possesses two functional homologues of
RT Escherichia coli endonuclease III.";
RL Biochemistry 37:6033-6040(1998).
RN [9]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=9545197; DOI=10.1016/s0960-9822(98)70158-7;
RA Bruner S.D., Nash H.M., Lane W.S., Verdine G.L.;
RT "Repair of oxidatively damaged guanine in Saccharomyces cerevisiae by an
RT alternative pathway.";
RL Curr. Biol. 8:393-403(1998).
RN [10]
RP FUNCTION, SUBSTRATES, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=9826748; DOI=10.1093/nar/26.23.5270;
RA Senturker S., Auffret van der Kemp P., You H.J., Doetsch P.W.,
RA Dizdaroglu M., Boiteux S.;
RT "Substrate specificities of the ntg1 and ntg2 proteins of Saccharomyces
RT cerevisiae for oxidized DNA bases are not identical.";
RL Nucleic Acids Res. 26:5270-5276(1998).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10471279; DOI=10.1021/bi991121i;
RA You H.J., Swanson R.L., Harrington C., Corbett A.H., Jinks-Robertson S.,
RA Sentuerker S., Wallace S.S., Boiteux S., Dizdaroglu M., Doetsch P.W.;
RT "Saccharomyces cerevisiae Ntg1p and Ntg2p: broad specificity N-glycosylases
RT for the repair of oxidative DNA damage in the nucleus and mitochondria.";
RL Biochemistry 38:11298-11306(1999).
RN [12]
RP FUNCTION IN OXIDATIVE DNA DAMAGE REPAIR, SUBCELLULAR LOCATION, DISRUPTION
RP PHENOTYPE, AND INDUCTION.
RX PubMed=10207101; DOI=10.1128/mcb.19.5.3779;
RA Alseth I., Eide L., Pirovano M., Rognes T., Seeberg E., Bjoras M.;
RT "The Saccharomyces cerevisiae homologues of endonuclease III from
RT Escherichia coli, Ntg1 and Ntg2, are both required for efficient repair of
RT spontaneous and induced oxidative DNA damage in yeast.";
RL Mol. Cell. Biol. 19:3779-3787(1999).
RN [13]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=14500818; DOI=10.1093/nar/gkg749;
RA Meadows K.L., Song B., Doetsch P.W.;
RT "Characterization of AP lyase activities of Saccharomyces cerevisiae Ntg1p
RT and Ntg2p: implications for biological function.";
RL Nucleic Acids Res. 31:5560-5567(2003).
RN [14]
RP FUNCTION IN DNA ALKYLATION DAMAGE REPAIR.
RX PubMed=14697759; DOI=10.1016/j.dnarep.2003.09.005;
RA Hanna M., Chow B.L., Morey N.J., Jinks-Robertson S., Doetsch P.W., Xiao W.;
RT "Involvement of two endonuclease III homologs in the base excision repair
RT pathway for the processing of DNA alkylation damage in Saccharomyces
RT cerevisiae.";
RL DNA Repair 3:51-59(2004).
RN [15]
RP DISRUPTION PHENOTYPE.
RX PubMed=15923634; DOI=10.1128/mcb.25.12.5196-5204.2005;
RA Doudican N.A., Song B., Shadel G.S., Doetsch P.W.;
RT "Oxidative DNA damage causes mitochondrial genomic instability in
RT Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 25:5196-5204(2005).
RN [16]
RP DISRUPTION PHENOTYPE.
RX PubMed=16730479; DOI=10.1016/j.dnarep.2006.04.002;
RA Phadnis N., Mehta R., Meednu N., Sia E.A.;
RT "Ntg1p, the base excision repair protein, generates mutagenic intermediates
RT in yeast mitochondrial DNA.";
RL DNA Repair 5:829-839(2006).
RN [17]
RP FUNCTION IN OXIDATIVE DNA DAMAGE REPAIR, AND SUBSTRATES.
RX PubMed=18983898; DOI=10.1016/j.bbagen.2008.10.001;
RA Gasparutto D., Muller E., Boiteux S., Cadet J.;
RT "Excision of the oxidatively formed 5-hydroxyhydantoin and 5-hydroxy-5-
RT methylhydantoin pyrimidine lesions by Escherichia coli and Saccharomyces
RT cerevisiae DNA N-glycosylases.";
RL Biochim. Biophys. Acta 1790:16-24(2009).
RN [18]
RP SUBCELLULAR LOCATION, SUMOYLATION, AND MUTAGENESIS OF LYS-364.
RX PubMed=19029246; DOI=10.1128/mcb.01357-08;
RA Griffiths L.M., Swartzlander D., Meadows K.L., Wilkinson K.D.,
RA Corbett A.H., Doetsch P.W.;
RT "Dynamic compartmentalization of base excision repair proteins in response
RT to nuclear and mitochondrial oxidative stress.";
RL Mol. Cell. Biol. 29:794-807(2009).
RN [19]
RP FUNCTION IN MTDNA REPLICATION.
RX PubMed=19074198; DOI=10.1093/nar/gkn993;
RA Hori A., Yoshida M., Shibata T., Ling F.;
RT "Reactive oxygen species regulate DNA copy number in isolated yeast
RT mitochondria by triggering recombination-mediated replication.";
RL Nucleic Acids Res. 37:749-761(2009).
RN [20]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP 3-LYS--LYS-6; 15-LYS-ARG-16; 33-LYS-ARG-34 AND LYS-243.
RX PubMed=20194111; DOI=10.1093/nar/gkq108;
RA Swartzlander D.B., Griffiths L.M., Lee J., Degtyareva N.P., Doetsch P.W.,
RA Corbett A.H.;
RT "Regulation of base excision repair: Ntg1 nuclear and mitochondrial dynamic
RT localization in response to genotoxic stress.";
RL Nucleic Acids Res. 38:3963-3974(2010).
CC -!- FUNCTION: Bifunctional DNA N-glycosylase with associated
CC apurinic/apyrimidinic (AP) lyase function that catalyzes the first step
CC in base excision repair (BER), the primary repair pathway for the
CC repair of oxidative DNA damage. The DNA N-glycosylase activity releases
CC the damaged DNA base from DNA by cleaving the N-glycosidic bond,
CC leaving an AP site. The AP-lyase activity cleaves the phosphodiester
CC bond 3' to the AP site by a beta-elimination. Primarily recognizes and
CC repairs oxidative base damage of pyrimidines, but also purine-derived
CC lesions, alkylation damage and cytosine photoproducts generated by UV
CC irradiation as well as abasic sites. Has also 8-oxoguanine DNA
CC glycosylase activity. The AP lyase can incise AP sites opposite all
CC four bases. May also play a role in the regulation of mtDNA copy number
CC by introducing a double-stranded break (DSB) at the mtDNA replication
CC origin ori5, initiating the rolling-circle mtDNA replication.
CC {ECO:0000255|HAMAP-Rule:MF_03183, ECO:0000269|PubMed:10207101,
CC ECO:0000269|PubMed:10471279, ECO:0000269|PubMed:14500818,
CC ECO:0000269|PubMed:14697759, ECO:0000269|PubMed:18983898,
CC ECO:0000269|PubMed:19074198, ECO:0000269|PubMed:20194111,
CC ECO:0000269|PubMed:8805338, ECO:0000269|PubMed:8855249,
CC ECO:0000269|PubMed:9020769, ECO:0000269|PubMed:9545197,
CC ECO:0000269|PubMed:9558341, ECO:0000269|PubMed:9826748}.
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_03183, ECO:0000269|PubMed:14500818,
CC ECO:0000269|PubMed:20194111, ECO:0000269|PubMed:9545197};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=227 nM for dihydrouracil containing duplex oligonucleotides (N-
CC glycosylase activity) {ECO:0000269|PubMed:14500818,
CC ECO:0000269|PubMed:9558341, ECO:0000269|PubMed:9826748};
CC KM=250 nM for 5-hydroxy-6-hydrothymine containing duplex
CC oligonucleotides (N-glycosylase activity)
CC {ECO:0000269|PubMed:14500818, ECO:0000269|PubMed:9558341,
CC ECO:0000269|PubMed:9826748};
CC KM=721 nM for 5-hydroxy-6-hydrouracil containing duplex
CC oligonucleotides (N-glycosylase activity)
CC {ECO:0000269|PubMed:14500818, ECO:0000269|PubMed:9558341,
CC ECO:0000269|PubMed:9826748};
CC KM=755 nM for 5-hydroxy-5-methylhydantoin containing duplex
CC oligonucleotides (N-glycosylase activity)
CC {ECO:0000269|PubMed:14500818, ECO:0000269|PubMed:9558341,
CC ECO:0000269|PubMed:9826748};
CC KM=997 nM for 5-hydroxyuracil containing duplex oligonucleotides (N-
CC glycosylase activity) {ECO:0000269|PubMed:14500818,
CC ECO:0000269|PubMed:9558341, ECO:0000269|PubMed:9826748};
CC KM=1380 nM for 5-hydroxycytosine containing duplex oligonucleotides
CC (N-glycosylase activity) {ECO:0000269|PubMed:14500818,
CC ECO:0000269|PubMed:9558341, ECO:0000269|PubMed:9826748};
CC KM=3250 nM for thymine glycol containing duplex oligonucleotides (N-
CC glycosylase activity) {ECO:0000269|PubMed:14500818,
CC ECO:0000269|PubMed:9558341, ECO:0000269|PubMed:9826748};
CC KM=1305 nM for 2,6-diamino-4-hydroxy-5-formamidopyrimidine (FapyAde)
CC containing duplex oligonucleotides (N-glycosylase activity)
CC {ECO:0000269|PubMed:14500818, ECO:0000269|PubMed:9558341,
CC ECO:0000269|PubMed:9826748};
CC KM=2460 nM for 4,6-diamino-5-formamidopyrimidine (FapyGua) containing
CC duplex oligonucleotides (N-glycosylase activity)
CC {ECO:0000269|PubMed:14500818, ECO:0000269|PubMed:9558341,
CC ECO:0000269|PubMed:9826748};
CC KM=24.86 nM for AP/G abasic-site containing duplex oligonucleotides
CC (AP lyase activity) {ECO:0000269|PubMed:14500818,
CC ECO:0000269|PubMed:9558341, ECO:0000269|PubMed:9826748};
CC KM=11.37 nM for AP/A abasic-site containing duplex oligonucleotides
CC (AP lyase activity) {ECO:0000269|PubMed:14500818,
CC ECO:0000269|PubMed:9558341, ECO:0000269|PubMed:9826748};
CC KM=6.67 nM for AP/T abasic-site containing duplex oligonucleotides
CC (AP lyase activity) {ECO:0000269|PubMed:14500818,
CC ECO:0000269|PubMed:9558341, ECO:0000269|PubMed:9826748};
CC KM=36.58 nM for AP/C abasic-site containing duplex oligonucleotides
CC (AP lyase activity) {ECO:0000269|PubMed:14500818,
CC ECO:0000269|PubMed:9558341, ECO:0000269|PubMed:9826748};
CC Vmax=1.9 nmol/min/ng enzyme for dihydrouracil containing duplex
CC oligonucleotides (N-glycosylase activity)
CC {ECO:0000269|PubMed:14500818, ECO:0000269|PubMed:9558341,
CC ECO:0000269|PubMed:9826748};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03183,
CC ECO:0000269|PubMed:10207101, ECO:0000269|PubMed:10471279,
CC ECO:0000269|PubMed:19029246, ECO:0000269|PubMed:20194111}.
CC Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03183,
CC ECO:0000269|PubMed:10207101, ECO:0000269|PubMed:10471279,
CC ECO:0000269|PubMed:19029246, ECO:0000269|PubMed:20194111}.
CC Note=Relocalizes to organelles containing elevated oxidative DNA
CC damage. {ECO:0000269|PubMed:19029246, ECO:0000269|PubMed:20194111}.
CC -!- INDUCTION: By oxidizing agents. {ECO:0000269|PubMed:10207101,
CC ECO:0000269|PubMed:8855249, ECO:0000269|PubMed:9558341}.
CC -!- PTM: Monosumoylated. Sumoylation is associated with targeting of NTG1
CC to nuclei containing oxidative DNA damage.
CC {ECO:0000269|PubMed:19029246}.
CC -!- DISRUPTION PHENOTYPE: Greatly increases spontaneous and hydrogen
CC peroxide-induced mutation frequency. Causes mitochondrial genome
CC instability. Suppresses mitochondrial point mutation rates, frameshifts
CC and recombination rates, probably because NTG1 can generate mutagenic
CC intermediates in yeast mitochondrial DNA. {ECO:0000269|PubMed:10207101,
CC ECO:0000269|PubMed:15923634, ECO:0000269|PubMed:16730479}.
CC -!- MISCELLANEOUS: Does not possess a consensus sequence for a C-terminal
CC iron-sulfur center typical of all other endonuclease III homologs.
CC {ECO:0000305|PubMed:9558341}.
CC -!- SIMILARITY: Belongs to the Nth/MutY family. {ECO:0000255|HAMAP-
CC Rule:MF_03183}.
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DR EMBL; L05146; AAC04942.1; -; Genomic_DNA.
DR EMBL; BK006935; DAA06973.1; -; Genomic_DNA.
DR PIR; S36719; S36719.
DR RefSeq; NP_009387.1; NM_001178160.1.
DR AlphaFoldDB; P31378; -.
DR SMR; P31378; -.
DR BioGRID; 31751; 112.
DR DIP; DIP-6614N; -.
DR IntAct; P31378; 24.
DR STRING; 4932.YAL015C; -.
DR iPTMnet; P31378; -.
DR MaxQB; P31378; -.
DR PaxDb; P31378; -.
DR PRIDE; P31378; -.
DR TopDownProteomics; P31378; -.
DR EnsemblFungi; YAL015C_mRNA; YAL015C; YAL015C.
DR GeneID; 851218; -.
DR KEGG; sce:YAL015C; -.
DR SGD; S000000013; NTG1.
DR VEuPathDB; FungiDB:YAL015C; -.
DR eggNOG; KOG1921; Eukaryota.
DR GeneTree; ENSGT00510000047513; -.
DR HOGENOM; CLU_012862_4_3_1; -.
DR InParanoid; P31378; -.
DR OMA; KLFKWVD; -.
DR BioCyc; YEAST:G3O-28827-MON; -.
DR PRO; PR:P31378; -.
DR Proteomes; UP000002311; Chromosome I.
DR RNAct; P31378; protein.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0140078; F:class I DNA-(apurinic or apyrimidinic site) endonuclease activity; IEA:UniProtKB-EC.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) endonuclease activity; IDA:SGD.
DR GO; GO:0008534; F:oxidized purine nucleobase lesion DNA N-glycosylase activity; IDA:SGD.
DR GO; GO:0000703; F:oxidized pyrimidine nucleobase lesion DNA N-glycosylase activity; IDA:SGD.
DR GO; GO:0006284; P:base-excision repair; IDA:SGD.
DR GO; GO:0006285; P:base-excision repair, AP site formation; IDA:SGD.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:SGD.
DR GO; GO:0006281; P:DNA repair; IDA:SGD.
DR GO; GO:0006296; P:nucleotide-excision repair, DNA incision, 5'-to lesion; IBA:GO_Central.
DR GO; GO:0090297; P:positive regulation of mitochondrial DNA replication; IMP:SGD.
DR CDD; cd00056; ENDO3c; 1.
DR Gene3D; 1.10.1670.10; -; 1.
DR HAMAP; MF_03183; Endonuclease_III_Nth; 1.
DR InterPro; IPR011257; DNA_glycosylase.
DR InterPro; IPR004036; Endonuclease-III-like_CS2.
DR InterPro; IPR003265; HhH-GPD_domain.
DR InterPro; IPR023170; HhH_base_excis_C.
DR InterPro; IPR000445; HhH_motif.
DR InterPro; IPR030841; NTH1.
DR Pfam; PF00633; HHH; 1.
DR Pfam; PF00730; HhH-GPD; 1.
DR SMART; SM00478; ENDO3c; 1.
DR SUPFAM; SSF48150; SSF48150; 1.
DR PROSITE; PS01155; ENDONUCLEASE_III_2; 1.
PE 1: Evidence at protein level;
KW DNA damage; DNA repair; Glycosidase; Hydrolase; Isopeptide bond; Lyase;
KW Mitochondrion; Nucleus; Reference proteome; Transit peptide;
KW Ubl conjugation.
FT TRANSIT 1..26
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03183"
FT CHAIN 27..399
FT /note="Endonuclease III homolog 1"
FT /id="PRO_0000001744"
FT DOMAIN 223..247
FT /note="HhH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03183"
FT MOTIF 14..37
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 243
FT /note="Nucleophile; for N-glycosylase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03183"
FT SITE 262
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03183"
FT CROSSLNK 194
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000305"
FT MUTAGEN 3..6
FT /note="KISK->EISE: In NTG1(mts); reduces mitochondrial
FT localization by 40%."
FT /evidence="ECO:0000269|PubMed:20194111"
FT MUTAGEN 15..16
FT /note="KR->AA: In NTG1(nls1); reduces nuclear localization
FT by 60%."
FT /evidence="ECO:0000269|PubMed:20194111"
FT MUTAGEN 33..34
FT /note="KR->AA: In NTG1(nls2); reduces nuclear localization
FT by 60%."
FT /evidence="ECO:0000269|PubMed:20194111"
FT MUTAGEN 243
FT /note="K->Q: Abolishes cleavage of substrate
FT oligonucleotides."
FT /evidence="ECO:0000269|PubMed:20194111"
FT MUTAGEN 364
FT /note="K->R: Cannot properly relocalize in response to
FT oxidative stress."
FT /evidence="ECO:0000269|PubMed:19029246"
SQ SEQUENCE 399 AA; 45577 MW; A3C878A3004908F3 CRC64;
MQKISKYSSM AILRKRPLVK TETGPESELL PEKRTKIKQE EVVPQPVDID WVKSLPNKQY
FEWIVVRNGN VPNRWATPLD PSILVTPAST KVPYKFQETY ARMRVLRSKI LAPVDIIGGS
SIPVTVASKC GISKEQISPR DYRLQVLLGV MLSSQTKDEV TAMAMLNIMR YCIDELHSEE
GMTLEAVLQI NETKLDELIH SVGFHTRKAK YILSTCKILQ DQFSSDVPAT INELLGLPGV
GPKMAYLTLQ KAWGKIEGIC VDVHVDRLTK LWKWVDAQKC KTPDQTRTQL QNWLPKGLWT
EINGLLVGFG QIITKSRNLG DMLQFLPPDD PRSSLDWDLQ SQLYKEIQQN IMSYPKWVKY
LEGKRELNVE AEINVKHEEK TVEETMVKLE NDISVKVED
