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Database: UniProt
Entry: A0A165A1M2_DAUCS
LinkDB: A0A165A1M2_DAUCS
Original site: A0A165A1M2_DAUCS 
ID   A0A165A1M2_DAUCS        Unreviewed;       380 AA.
AC   A0A165A1M2;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Fe2OG dioxygenase domain-containing protein {ECO:0000259|PROSITE:PS51471};
GN   ORFNames=DCAR_015874 {ECO:0000313|EMBL:KZM96764.1};
OS   Daucus carota subsp. sativus (Carrot).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Apiales; Apiaceae; Apioideae; Scandiceae; Daucinae;
OC   Daucus; Daucus sect. Daucus.
OX   NCBI_TaxID=79200 {ECO:0000313|EMBL:KZM96764.1};
RN   [1] {ECO:0000313|EMBL:KZM96764.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Leaf {ECO:0000313|EMBL:KZM96764.1};
RX   PubMed=27158781; DOI=10.1038/ng.3565;
RA   Iorizzo M., Ellison S., Senalik D., Zeng P., Satapoomin P., Huang J.,
RA   Bowman M., Iovene M., Sanseverino W., Cavagnaro P., Yildiz M.,
RA   Macko-Podgorni A., Moranska E., Grzebelus E., Grzebelus D., Ashrafi H.,
RA   Zheng Z., Cheng S., Spooner D., Van Deynze A., Simon P.;
RT   "A high-quality carrot genome assembly provides new insights into
RT   carotenoid accumulation and asterid genome evolution.";
RL   Nat. Genet. 48:657-666(2016).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 2-oxoglutarate + gibberellin A12 + H(+) + 3 O2 = 3 CO2 +
CC         gibberellin A9 + 2 H2O + 2 succinate; Xref=Rhea:RHEA:60772,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031,
CC         ChEBI:CHEBI:58627, ChEBI:CHEBI:73255;
CC         Evidence={ECO:0000256|ARBA:ARBA00043814};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60773;
CC         Evidence={ECO:0000256|ARBA:ARBA00043814};
CC   -!- COFACTOR:
CC       Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC         Evidence={ECO:0000256|ARBA:ARBA00001961};
CC   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family. GA20OX subfamily. {ECO:0000256|ARBA:ARBA00043997}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KZM96764.1}.
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DR   EMBL; LNRQ01000004; KZM96764.1; -; Genomic_DNA.
DR   RefSeq; XP_017246239.1; XM_017390750.1.
DR   AlphaFoldDB; A0A165A1M2; -.
DR   STRING; 79200.A0A165A1M2; -.
DR   EnsemblPlants; KZM96764; KZM96764; DCAR_015874.
DR   GeneID; 108217856; -.
DR   Gramene; KZM96764; KZM96764; DCAR_015874.
DR   KEGG; dcr:108217856; -.
DR   OMA; DEYENFG; -.
DR   OrthoDB; 1057251at2759; -.
DR   Proteomes; UP000077755; Chromosome 4.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; 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:SF53; GIBBERELLIN 20 OXIDASE 1; 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:UP000077755}.
FT   DOMAIN          222..322
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
SQ   SEQUENCE   380 AA;  43216 MW;  DAE397CC002B491F CRC64;
     MAASQSSRPL HFQHSYEDNN HHSQVVFDAS IIQKETTIPK EFIWPDHEKP SLNTQELKVP
     LIDLGAFLSG DPSAAKESSI LIGQACEEHG FFMVVNHGVD TNLISDAHKF MNLFFDLPLY
     VKQKAQRKLG ENFGYASSFT GRFASKLPWK ETFSFQYCAD ERMSSTTVED YFTNKFGPDF
     AKPGKVYQDY SHAMSTLSLK IMGLLEISLG VSRSHFKNLF EDHDSIVRLN YYPPCQKPEL
     TLGTGPHSDP TSLTILHQDH VAGLEVLVDD QWRCILPNTS AFVINIGDTL MAMTNGRYKS
     CLHRAVVNNE TARKSIAFFL CPRKDKVVIP PAELVDQKNP RSYPDFTWAE LLQFTQMHYR
     ADMNTLDAFS TWLLTKNNRE
//
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