ALKB2_ARATH
ID ALKB2_ARATH Reviewed; 314 AA.
AC Q9SIE0;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=DNA oxidative demethylase ALKBH2;
DE EC=1.14.11.33;
DE AltName: Full=Alkylated DNA repair protein alkB homolog 2;
DE AltName: Full=Alpha-ketoglutarate-dependent dioxygenase alkB homolog 2;
GN Name=ALKBH2; OrderedLocusNames=At2g22260; ORFNames=T26C19.8;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=22532610; DOI=10.1093/nar/gks327;
RA Meza T.J., Moen M.N., Vagbo C.B., Krokan H.E., Klungland A., Grini P.E.,
RA Falnes P.O.;
RT "The DNA dioxygenase ALKBH2 protects Arabidopsis thaliana against
RT methylation damage.";
RL Nucleic Acids Res. 40:6620-6631(2012).
CC -!- FUNCTION: Dioxygenase that repairs alkylated DNA containing 1-
CC methyladenine and 1-ethenoadenine by oxidative demethylation. Accepts
CC double-stranded and single-stranded substrates, with a preference for
CC dsDNA over ssDNA. Confers resistance to methylating agents such as
CC methylmethanesulphonate (MMS). {ECO:0000269|PubMed:22532610}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + a methylated nucleobase within DNA + O2 = a
CC nucleobase within DNA + CO2 + formaldehyde + succinate;
CC Xref=Rhea:RHEA:30299, Rhea:RHEA-COMP:12192, Rhea:RHEA-COMP:12193,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:16842, ChEBI:CHEBI:30031, ChEBI:CHEBI:32875,
CC ChEBI:CHEBI:64428; EC=1.14.11.33;
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00805};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00805};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously, including in seedlings,
CC leaves and flowers. {ECO:0000269|PubMed:22532610}.
CC -!- DEVELOPMENTAL STAGE: In seedlings, mostly present in the shoot
CC meristematic region, as well as in the vasculature of the hypocotyl and
CC root. Expressed in both primary and lateral root vasculature. In
CC flowers, accumulates in sepals, stem, carpel tissue and anther
CC filaments. {ECO:0000269|PubMed:22532610}.
CC -!- DISRUPTION PHENOTYPE: Enhanced sensitivity to the methylating agent
CC methylmethanesulphonate (MMS) leading to abnormal seedlings in presence
CC of MMS. {ECO:0000269|PubMed:22532610}.
CC -!- SIMILARITY: Belongs to the alkB family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AY089037; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AC007168; AAD23616.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC07286.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62872.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62873.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62874.1; -; Genomic_DNA.
DR EMBL; AY089037; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; F84610; F84610.
DR RefSeq; NP_001324998.1; NM_001335789.1.
DR RefSeq; NP_001324999.1; NM_001335788.1.
DR RefSeq; NP_001325000.1; NM_001335786.1.
DR RefSeq; NP_565530.1; NM_127792.4.
DR AlphaFoldDB; Q9SIE0; -.
DR SMR; Q9SIE0; -.
DR STRING; 3702.AT2G22260.1; -.
DR PaxDb; Q9SIE0; -.
DR PRIDE; Q9SIE0; -.
DR ProteomicsDB; 244955; -.
DR DNASU; 816759; -.
DR EnsemblPlants; AT2G22260.1; AT2G22260.1; AT2G22260.
DR EnsemblPlants; AT2G22260.2; AT2G22260.2; AT2G22260.
DR EnsemblPlants; AT2G22260.4; AT2G22260.4; AT2G22260.
DR EnsemblPlants; AT2G22260.5; AT2G22260.5; AT2G22260.
DR GeneID; 816759; -.
DR Gramene; AT2G22260.1; AT2G22260.1; AT2G22260.
DR Gramene; AT2G22260.2; AT2G22260.2; AT2G22260.
DR Gramene; AT2G22260.4; AT2G22260.4; AT2G22260.
DR Gramene; AT2G22260.5; AT2G22260.5; AT2G22260.
DR KEGG; ath:AT2G22260; -.
DR Araport; AT2G22260; -.
DR TAIR; locus:2060430; AT2G22260.
DR eggNOG; ENOG502QW9E; Eukaryota.
DR HOGENOM; CLU_048788_3_0_1; -.
DR InParanoid; Q9SIE0; -.
DR PhylomeDB; Q9SIE0; -.
DR PRO; PR:Q9SIE0; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SIE0; baseline and differential.
DR Genevisible; Q9SIE0; AT.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0051747; F:cytosine C-5 DNA demethylase activity; IBA:GO_Central.
DR GO; GO:0035514; F:DNA demethylase activity; IDA:TAIR.
DR GO; GO:0043734; F:DNA-N1-methyladenine dioxygenase activity; IBA:GO_Central.
DR GO; GO:0008198; F:ferrous iron binding; IBA:GO_Central.
DR GO; GO:0035516; F:oxidative DNA demethylase activity; IEA:UniProtKB-EC.
DR GO; GO:0006307; P:DNA dealkylation involved in DNA repair; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; IDA:TAIR.
DR GO; GO:0035511; P:oxidative DNA demethylation; IBA:GO_Central.
DR Gene3D; 2.60.120.590; -; 1.
DR InterPro; IPR027450; AlkB-like.
DR InterPro; IPR037151; AlkB-like_sf.
DR InterPro; IPR032852; ALKBH2.
DR InterPro; IPR025131; DUF4057.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR PANTHER; PTHR31573; PTHR31573; 1.
DR Pfam; PF13532; 2OG-FeII_Oxy_2; 1.
DR Pfam; PF13266; DUF4057; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 2: Evidence at transcript level;
KW Dioxygenase; DNA damage; DNA repair; Iron; Metal-binding; Nucleus;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..314
FT /note="DNA oxidative demethylase ALKBH2"
FT /id="PRO_0000426011"
FT DOMAIN 194..314
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT REGION 1..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 242..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..74
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 132
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 160..163
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 201..203
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250"
FT BINDING 213
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 215
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 216
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 293
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 305..311
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250"
FT BINDING 305
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT CONFLICT 189
FT /note="V -> A (in Ref. 3; AY089037)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 314 AA; 35515 MW; 0106C31C54D8DC43 CRC64;
MTNPLNSTAA NRSNQPSSDG ISDGQITNEE AESLINKKNC SGHKLKEVTD SDTFSDNGKD
DSDTKKRFHY HQDQRRMSLT SIVAVESPSS SNAPSRKTID LGHGSDLIYI QRFLPFQQSW
TFFDYLDKHI PWTRPTIRVF GRSCLQPRDT CYVASSGLTA LVYSGYRPTS YSWDDFPPLK
EILDAIYKVL PGSRFNSLLL NRYKGASDYV AWHADDEKIY GPTPEIASVS FGCERDFVLK
KKKDEESSQG KTGDSGPAKK RLKRSSREDQ QSLTLKHGSL LVMRGYTQRD WIHSVPKRAK
AEGTRINLTF RLVL
