ID M0ZQM8_SOLTU Unreviewed; 301 AA.
AC M0ZQM8;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=ACC oxidase {ECO:0000313|EnsemblPlants:PGSC0003DMT400005971};
GN Name=102577542 {ECO:0000313|EnsemblPlants:PGSC0003DMT400005971};
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:PGSC0003DMT400005971, 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:PGSC0003DMT400005971}
RP IDENTIFICATION.
RC STRAIN=DM1-3 516 R44 {ECO:0000313|EnsemblPlants:PGSC0003DMT400005971};
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; NP_001275149.2; NM_001288220.2.
DR AlphaFoldDB; M0ZQM8; -.
DR SMR; M0ZQM8; -.
DR STRING; 4113.M0ZQM8; -.
DR PaxDb; 4113-PGSC0003DMT400005971; -.
DR EnsemblPlants; PGSC0003DMT400005971; PGSC0003DMT400005971; PGSC0003DMG400002321.
DR GeneID; 102577542; -.
DR Gramene; PGSC0003DMT400005971; PGSC0003DMT400005971; PGSC0003DMG400002321.
DR KEGG; sot:102577542; -.
DR eggNOG; KOG0143; Eukaryota.
DR HOGENOM; CLU_010119_16_1_1; -.
DR InParanoid; M0ZQM8; -.
DR OMA; YPQCPHP; -.
DR OrthoDB; 1057251at2759; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; M0ZQM8; 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; PTHR47991:SF93; 1-AMINOCYCLOPROPANE-1-CARBOXYLATE OXIDASE 1; 1.
DR PANTHER; PTHR47991; OXOGLUTARATE/IRON-DEPENDENT DIOXYGENASE; 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:UP000011115};
KW Vitamin C {ECO:0000256|ARBA:ARBA00022896}.
FT DOMAIN 149..252
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
SQ SEQUENCE 301 AA; 34314 MW; EA9850B49662CF4C CRC64;
MEIPVIDFSK LEGEERSATM SLLHQACEKW GFFMIENHGI DTYLMDNVKQ LVNQHYEANM
KKRFYESELP MSLEKKGNIS NTDWESTFFV WHRPTSNIYE IQGLSKELCK AVDDYIDQLI
ELAENLSELM CENLGLEKSC IKEAFSGSKG PSVGTKVAIY PQCPRPDLVR GLREHTDAGG
IILLLQDEQV PGLEFFKDGH WVNIPPSKNN RLFVNIGDQI EILSNGMYKS IRHRVMAEKD
GNRLSIATFY NPAGEAIISP APKLLYPCHL RFQDYLNLYS KTKFAEKGPR FESAKTLANG
H
//