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
//