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Database: UniProt
Entry: D7LN10_ARALL
LinkDB: D7LN10_ARALL
Original site: D7LN10_ARALL 
ID   D7LN10_ARALL            Unreviewed;       331 AA.
AC   D7LN10;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   SubName: Full=Oxidoreductase {ECO:0000313|EMBL:EFH52045.1};
GN   ORFNames=ARALYDRAFT_485020 {ECO:0000313|EMBL:EFH52045.1};
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|RuleBase:RU003682}.
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DR   EMBL; GL348717; EFH52045.1; -; Genomic_DNA.
DR   RefSeq; XP_002875786.1; XM_002875740.1.
DR   AlphaFoldDB; D7LN10; -.
DR   STRING; 81972.D7LN10; -.
DR   EnsemblPlants; fgenesh2_kg.5__1012__AT3G46490.1; fgenesh2_kg.5__1012__AT3G46490.1; fgenesh2_kg.5__1012__AT3G46490.1.
DR   GeneID; 9313557; -.
DR   Gramene; fgenesh2_kg.5__1012__AT3G46490.1; fgenesh2_kg.5__1012__AT3G46490.1; fgenesh2_kg.5__1012__AT3G46490.1.
DR   KEGG; aly:9313557; -.
DR   eggNOG; KOG0143; Eukaryota.
DR   HOGENOM; CLU_010119_6_5_1; -.
DR   OrthoDB; 101125at2759; -.
DR   Proteomes; UP000008694; Unassembled WGS sequence.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:UniProt.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
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; PTHR10209:SF895; 2-OXOGLUTARATE (2OG) AND FE(II)-DEPENDENT OXYGENASE SUPERFAMILY PROTEIN; 1.
DR   PANTHER; PTHR10209; OXIDOREDUCTASE, 2OG-FE II OXYGENASE FAMILY PROTEIN; 1.
DR   Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR   Pfam; PF14226; DIOX_N; 1.
DR   PRINTS; PR00682; IPNSYNTHASE.
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          183..287
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
SQ   SEQUENCE   331 AA;  37601 MW;  FCD29716D4DA38E2 CRC64;
     MENKTEEDKV SIIKVSALTC IDLDNSNLHQ SAVLLKQACL DSGFFYVINH GISEELKDEA
     FEQSKKFFAL PLEEKMKVLR NEKYRGYAPF HDSLLDPKNQ FRGDYKEGFT IGFEGGKDGP
     HGDKPFHSPN IWPNSDVLPG WRETMEKYYQ EALRVCKSIA RIMALALDLD VDYFNTPEML
     GNPIADMVLF HYEGKSDPSK GIYACGAHSD FGMMSLLATD GVMGLQICKD KDVMPQKWEY
     IPSLKGAYIV NLGDLLERWN NGYFKSTLHR VLGNGQDRYS IPFFLKPSHD CIIECLPNCQ
     SENNLPKYPA IKCSTYISPR YKAAHAHLKQ T
//
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