ID D7L6Y7_ARALL Unreviewed; 310 AA.
AC D7L6Y7;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Fe2OG dioxygenase domain-containing protein {ECO:0000259|PROSITE:PS51471};
GN ORFNames=ARALYDRAFT_343239 {ECO:0000313|EMBL:EFH60241.1};
OS Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN [1] {ECO:0000313|Proteomes:UP000008694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX PubMed=21478890; DOI=10.1038/ng.807;
RA Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT change.";
RL Nat. Genet. 43:476-481(2011).
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000256|ARBA:ARBA00008056, ECO:0000256|RuleBase:RU003682}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GL348715; EFH60241.1; -; Genomic_DNA.
DR RefSeq; XP_002883982.1; XM_002883936.1.
DR AlphaFoldDB; D7L6Y7; -.
DR STRING; 81972.D7L6Y7; -.
DR EnsemblPlants; fgenesh1_pg.C_scaffold_3003002; fgenesh1_pg.C_scaffold_3003002; fgenesh1_pg.C_scaffold_3003002.
DR GeneID; 9320049; -.
DR Gramene; fgenesh1_pg.C_scaffold_3003002; fgenesh1_pg.C_scaffold_3003002; fgenesh1_pg.C_scaffold_3003002.
DR KEGG; aly:9320049; -.
DR eggNOG; KOG0143; Eukaryota.
DR HOGENOM; CLU_010119_16_1_1; -.
DR OrthoDB; 1057251at2759; -.
DR Proteomes; UP000008694; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0071398; P:cellular response to fatty acid; IEA:EnsemblPlants.
DR GO; GO:0071732; P:cellular response to nitric oxide; IEA:EnsemblPlants.
DR GO; GO:0051365; P:cellular response to potassium ion starvation; IEA:EnsemblPlants.
DR InterPro; IPR026992; DIOX_N.
DR InterPro; IPR044861; IPNS-like_FE2OG_OXY.
DR InterPro; IPR027443; IPNS-like_sf.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR PANTHER; PTHR47991:SF93; 1-AMINOCYCLOPROPANE-1-CARBOXYLATE OXIDASE 1; 1.
DR PANTHER; PTHR47991; OXOGLUTARATE/IRON-DEPENDENT DIOXYGENASE; 1.
DR Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR Pfam; PF14226; DIOX_N; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU003682};
KW Metal-binding {ECO:0000256|RuleBase:RU003682};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003682};
KW Reference proteome {ECO:0000313|Proteomes:UP000008694}.
FT DOMAIN 158..259
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
SQ SEQUENCE 310 AA; 35320 MW; D77B515958659A4A CRC64;
MVLIKEREME IPVIDFGELD GENRSKTMSL LDHACDKWGF FMVDNHGIDK ELMEKVKKMI
NSYYEEHLKE KFYQSEMVKA LSEGKTSDAD WESSFFISHK PTSNFCEILN ISVERSKTMD
EYVCQLHKFA ERLSKLMSEN LGLDQEYIMN AFSGSKGPAF GTKVAKYPEC PRPELMRGLR
EHTDAGGIIL LLQDDQVPGL EFFKDGKWFP IPPSKNNTIF VNTGDQLEIL SNGRYKSVVH
RVMTVKHGSR LSIATFYNPA GDAIISPAPK LLYPSGYRFQ DYLKLYSTTK FGDKGPRLES
MKKMGNADSA
//
