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Database: UniProt
Entry: A0A3Q7EZ79_SOLLC
LinkDB: A0A3Q7EZ79_SOLLC
Original site: A0A3Q7EZ79_SOLLC 
ID   A0A3Q7EZ79_SOLLC        Unreviewed;       350 AA.
AC   A0A3Q7EZ79;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Fe2OG dioxygenase domain-containing protein {ECO:0000259|PROSITE:PS51471};
OS   Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC   Solanum subgen. Lycopersicon.
OX   NCBI_TaxID=4081 {ECO:0000313|EnsemblPlants:Solyc02g062470.2.1};
RN   [1] {ECO:0000313|EnsemblPlants:Solyc02g062470.2.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Heinz 1706 {ECO:0000313|EnsemblPlants:Solyc02g062470.2.1};
RX   PubMed=22660326; DOI=10.1038/nature11119;
RG   Tomato Genome Consortium;
RT   "The tomato genome sequence provides insights into fleshy fruit
RT   evolution.";
RL   Nature 485:635-641(2012).
RN   [2] {ECO:0000313|EnsemblPlants:Solyc02g062470.2.1}
RP   IDENTIFICATION.
RC   STRAIN=cv. Heinz 1706 {ECO:0000313|EnsemblPlants:Solyc02g062470.2.1};
RG   EnsemblPlants;
RL   Submitted (JAN-2019) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family. {ECO:0000256|ARBA:ARBA00008056, ECO:0000256|RuleBase:RU003682}.
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DR   AlphaFoldDB; A0A3Q7EZ79; -.
DR   STRING; 4081.A0A3Q7EZ79; -.
DR   PaxDb; 4081-Solyc02g062490-2-1; -.
DR   EnsemblPlants; Solyc02g062470.2.1; Solyc02g062470.2.1; Solyc02g062470.2.
DR   Gramene; Solyc02g062470.2.1; Solyc02g062470.2.1; Solyc02g062470.2.
DR   InParanoid; A0A3Q7EZ79; -.
DR   OMA; INRSDTH; -.
DR   Proteomes; UP000004994; Chromosome 2.
DR   GO; GO:0016706; F:2-oxoglutarate-dependent dioxygenase activity; IBA:GO_Central.
DR   GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009805; P:coumarin biosynthetic process; IEA:UniProt.
DR   GO; GO:0002238; P:response to molecule of fungal origin; 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; PTHR47990; 2-OXOGLUTARATE (2OG) AND FE(II)-DEPENDENT OXYGENASE SUPERFAMILY PROTEIN-RELATED; 1.
DR   PANTHER; PTHR47990:SF100; FE2OG DIOXYGENASE DOMAIN-CONTAINING PROTEIN; 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:UP000004994};
KW   Vitamin C {ECO:0000256|ARBA:ARBA00022896}.
FT   DOMAIN          191..297
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
SQ   SEQUENCE   350 AA;  39739 MW;  756052F1C1907468 CRC64;
     MASTKLVKVP TIDFSNHQDL KPNTPLWESK KIQVFEALQE YGCFEAIYDK VPKDIREETF
     SISKEIFEFP LETKLKNISE KPTHGYMGMI PQLPLYESLC IPDLLNPKSL QSFANIFWPQ
     GNQHFWYVYL CFYFALAEVF KKVEIVLLLS TPFARNLVKS YSNPLLELDE MLKRMISENL
     GLKNHIDELL NANYILFRFT QYKGSSIASG DENNKAAGLG GHTDGNFLSI ISQNEVNGLQ
     INKNGEWIDV NISPNSYVVL SGDSFTAWTN GRLHSPVHRV EMPRGSDRYS IQLFSLSKPG
     HFIEAPKEMV DEEHPLLFKP FEILGLLGYG ATEAGYTTPP SDLFKAYCGV
//
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