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Database: UniProt
Entry: D7L968_ARALL
LinkDB: D7L968_ARALL
Original site: D7L968_ARALL 
ID   D7L968_ARALL            Unreviewed;       352 AA.
AC   D7L968;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   SubName: Full=Oxidoreductase {ECO:0000313|EMBL:EFH61547.1};
GN   ORFNames=ARALYDRAFT_479417 {ECO:0000313|EMBL:EFH61547.1};
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; GL348715; EFH61547.1; -; Genomic_DNA.
DR   RefSeq; XP_002885288.1; XM_002885242.1.
DR   AlphaFoldDB; D7L968; -.
DR   EnsemblPlants; fgenesh2_kg.3__2118__AT3G19000.1; fgenesh2_kg.3__2118__AT3G19000.1; fgenesh2_kg.3__2118__AT3G19000.1.
DR   Gramene; fgenesh2_kg.3__2118__AT3G19000.1; fgenesh2_kg.3__2118__AT3G19000.1; fgenesh2_kg.3__2118__AT3G19000.1.
DR   eggNOG; KOG0143; Eukaryota.
DR   HOGENOM; CLU_010119_16_3_1; -.
DR   OrthoDB; 1057251at2759; -.
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:SF850; 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          198..299
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
SQ   SEQUENCE   352 AA;  40624 MW;  03DC0985CC4B2CB7 CRC64;
     MGELDEAFIQ APEHRPNTHL TNSNDFIYSD EIPTIDLSSL RDPDHDKTAI AAEIAEACKR
     WGFFQVINHG LPSDLRRRVE EACAEFFNLT TEEKRKVKRD EVNPMGYHDE EHTKNVRDWK
     EIFDFFLQDS TIVPATPEPE DTELRKLTNQ WPQNPSHFRE ACQEYAREVE KLAFRLLELV
     SISLGLPGDR LTGFFNEQTS FLRFNHYPPC PNPELALGVG RHKDGGALTV LAQDSVGGLQ
     VSRRSDGQWI PVKPISDALI INIGNCIQVW TNDKYWSAEH RVVVNTSKER FSIPFFFFPS
     HEANIAPLEE LISEENPPCY KTYNWGKFFV SRNRSDFKKL EVENIQIDHF KA
//
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