ID M1CG17_SOLTU Unreviewed; 351 AA.
AC M1CG17;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=2-oxoglutarate-dependent dioxygenase {ECO:0000313|EnsemblPlants:PGSC0003DMT400066714};
GN Name=102589984 {ECO:0000313|EnsemblPlants:PGSC0003DMT400066714};
OS Solanum tuberosum (Potato).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4113 {ECO:0000313|EnsemblPlants:PGSC0003DMT400066714, ECO:0000313|Proteomes:UP000011115};
RN [1] {ECO:0000313|Proteomes:UP000011115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DM1-3 516 R44 {ECO:0000313|Proteomes:UP000011115};
RX PubMed=21743474; DOI=10.1038/nature10158;
RG The Potato Genome Sequencing Consortium;
RT "Genome sequence and analysis of the tuber crop potato.";
RL Nature 475:189-195(2011).
RN [2] {ECO:0000313|EnsemblPlants:PGSC0003DMT400066714}
RP IDENTIFICATION.
RC STRAIN=DM1-3 516 R44 {ECO:0000313|EnsemblPlants:PGSC0003DMT400066714};
RG EnsemblPlants;
RL Submitted (JUN-2015) 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 RefSeq; XP_006346491.1; XM_006346429.2.
DR AlphaFoldDB; M1CG17; -.
DR PaxDb; 4113-PGSC0003DMT400066714; -.
DR EnsemblPlants; PGSC0003DMT400066714; PGSC0003DMT400066714; PGSC0003DMG402025923.
DR GeneID; 102589984; -.
DR Gramene; PGSC0003DMT400066714; PGSC0003DMT400066714; PGSC0003DMG402025923.
DR KEGG; sot:102589984; -.
DR eggNOG; KOG0143; Eukaryota.
DR HOGENOM; CLU_010119_16_3_1; -.
DR InParanoid; M1CG17; -.
DR OMA; WIQPLEE; -.
DR OrthoDB; 1057251at2759; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; M1CG17; baseline.
DR GO; GO:0016706; F:2-oxoglutarate-dependent dioxygenase activity; IEA:UniProt.
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; PTHR10209; OXIDOREDUCTASE, 2OG-FE II OXYGENASE FAMILY PROTEIN; 1.
DR PANTHER; PTHR10209:SF690; PROTEIN DMR6-LIKE OXYGENASE 2-LIKE; 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:UP000011115};
KW Vitamin C {ECO:0000256|ARBA:ARBA00022896}.
FT DOMAIN 197..298
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT REGION 332..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 351 AA; 40601 MW; B51F0166A9CEFD14 CRC64;
MVIVHPAIIQ DVEHRPKLTK TEAEGIPVID LSILNCPYTS TTDAELESLV AEIRNACKKW
GFFQVINHGV SLECREKIEL ASRKFFGLPK EEKIKVKRNE VNFMGYYDTE LTKKIRDWKE
VFDFTVEKTA MVPLSQDPND KELREFHNQW PQYPPGLREV CEEYIQQMQK LAYKLAEVIS
LSLSLPAKRL NEFFEDQVAF GRINHYPPCP VPHLALGVGR HKDAGLFTIL SQDDTGGLEI
KRKTDGEWIG VKPTPDAYIV NLGDATQVYS NGEYESVEHR VVLNTERSRF SIPFFVNPSH
STWIQPLEEK VNEKNPAKYK AYNWGMLYTH RRKHDPKTRD EENLPVDHFK A
//
