ID R0INR7_9BRAS Unreviewed; 469 AA.
AC R0INR7;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Fe2OG dioxygenase domain-containing protein {ECO:0000259|PROSITE:PS51471};
GN ORFNames=CARUB_v10009046mg {ECO:0000313|EMBL:EOA40320.1};
OS Capsella rubella.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Capsella.
OX NCBI_TaxID=81985 {ECO:0000313|EMBL:EOA40320.1, ECO:0000313|Proteomes:UP000029121};
RN [1] {ECO:0000313|Proteomes:UP000029121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Monte Gargano {ECO:0000313|Proteomes:UP000029121};
RX PubMed=23749190; DOI=10.1038/ng.2669;
RA Slotte T., Hazzouri K.M., Agren J.A., Koenig D., Maumus F., Guo Y.L.,
RA Steige K., Platts A.E., Escobar J.S., Newman L.K., Wang W., Mandakova T.,
RA Vello E., Smith L.M., Henz S.R., Steffen J., Takuno S., Brandvain Y.,
RA Coop G., Andolfatto P., Hu T.T., Blanchette M., Clark R.M., Quesneville H.,
RA Nordborg M., Gaut B.S., Lysak M.A., Jenkins J., Grimwood J., Chapman J.,
RA Prochnik S., Shu S., Rokhsar D., Schmutz J., Weigel D., Wright S.I.;
RT "The Capsella rubella genome and the genomic consequences of rapid mating
RT system evolution.";
RL Nat. Genet. 45:831-835(2013).
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000256|RuleBase:RU003682}.
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DR EMBL; KB870805; EOA40320.1; -; Genomic_DNA.
DR RefSeq; XP_006307422.1; XM_006307360.1.
DR AlphaFoldDB; R0INR7; -.
DR STRING; 81985.R0INR7; -.
DR eggNOG; KOG0143; Eukaryota.
DR Proteomes; UP000029121; 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:SF865; 1-AMINOCYCLOPROPANE-1-CARBOXYLATE OXIDASE HOMOLOG 4; 1.
DR PANTHER; PTHR10209; OXIDOREDUCTASE, 2OG-FE II OXYGENASE FAMILY PROTEIN; 1.
DR Pfam; PF03171; 2OG-FeII_Oxy; 2.
DR Pfam; PF14226; DIOX_N; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 2.
DR PROSITE; PS51471; FE2OG_OXY; 2.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
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:UP000029121}.
FT DOMAIN 36..203
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT DOMAIN 317..422
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT COILED 100..127
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 469 AA; 52515 MW; D4733ECB2CEA4904 CRC64;
MEYSKELLNL GELVYELLSE ALGVDSDYLK DMDCAKSQFI VGQYYPPCPQ PDLAIGINKH
TDSSFITILL QDNIGGLQVL YDSQYWVDVS PIPGALVINI GDLLQKKREE KNRAEEAMES
IDSSSQAKAF DETQIGVKGL VDSGIKEIPE MFRATQATLA SFKSPPPPKH LTIPTIDLKG
GSVVEKIRGA AERWGLFQVV NHGIPVEVLD RMIQGMRSFH EQEPEAKKRF YSRDHTRDVI
YYSNFDLYNS ESASWRDTLG CYTAPEPPLL EDLPSVCGEV ILEYSKEIMN LGELLFERLS
EALGLDSHHL KDMGCAKSQY VAGQYYPPCP QPDLTIGLNK HTDISFITIL LQDNIGGLQV
LYDGQYWVDV TPVPGALVIN IGDFLQLISN DKFKSAEHRV IANGSSEPRT SVVSVFSTFM
RASSRVYGPI KNLVSKENPA KYRDFTLTEF STIFGSKKID TPKLHHFRI
//
