ID B9SIK9_RICCO Unreviewed; 362 AA.
AC B9SIK9;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=feruloyl-CoA 6-hydroxylase {ECO:0000256|ARBA:ARBA00012885};
DE EC=1.14.11.61 {ECO:0000256|ARBA:ARBA00012885};
GN ORFNames=RCOM_0822300 {ECO:0000313|EMBL:EEF36522.1};
OS Ricinus communis (Castor bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC Ricinus.
OX NCBI_TaxID=3988 {ECO:0000313|Proteomes:UP000008311};
RN [1] {ECO:0000313|Proteomes:UP000008311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Hale {ECO:0000313|Proteomes:UP000008311};
RX PubMed=20729833; DOI=10.1038/nbt.1674;
RA Chan A.P., Crabtree J., Zhao Q., Lorenzi H., Orvis J., Puiu D.,
RA Melake-Berhan A., Jones K.M., Redman J., Chen G., Cahoon E.B., Gedil M.,
RA Stanke M., Haas B.J., Wortman J.R., Fraser-Liggett C.M., Ravel J.,
RA Rabinowicz P.D.;
RT "Draft genome sequence of the oilseed species Ricinus communis.";
RL Nat. Biotechnol. 28:951-956(2010).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-feruloyl-CoA + 2-oxoglutarate + O2 = (E)-6-
CC hydroxyferuloyl-CoA + CO2 + succinate; Xref=Rhea:RHEA:57856,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:87305, ChEBI:CHEBI:142390;
CC EC=1.14.11.61; Evidence={ECO:0000256|ARBA:ARBA00000471};
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. {ECO:0000256|RuleBase:RU003682}.
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DR EMBL; EQ973975; EEF36522.1; -; Genomic_DNA.
DR RefSeq; XP_002525828.1; XM_002525782.1.
DR AlphaFoldDB; B9SIK9; -.
DR STRING; 3988.B9SIK9; -.
DR GeneID; 8282976; -.
DR KEGG; rcu:8282976; -.
DR eggNOG; KOG0143; Eukaryota.
DR InParanoid; B9SIK9; -.
DR Proteomes; UP000008311; Unassembled WGS sequence.
DR GO; GO:0102312; F:4-coumaroyl 2'-hydroxylase activity; IEA:RHEA.
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:SF243; FERULOYL COA ORTHO-HYDROXYLASE 1-RELATED; 1.
DR PANTHER; PTHR10209; OXIDOREDUCTASE, 2OG-FE II OXYGENASE FAMILY 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 Dioxygenase {ECO:0000313|EMBL:EEF36522.1};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU003682};
KW Metal-binding {ECO:0000256|RuleBase:RU003682};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003682,
KW ECO:0000313|EMBL:EEF36522.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008311}.
FT DOMAIN 201..313
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
SQ SEQUENCE 362 AA; 40313 MW; 658A830D2BD5367F CRC64;
MAPTLAESAP HSSFDLNDFV INKGNGVKGL SDLGLKSLPR QYIQPQEALI NIIPQDSIPV
IDMSNFDNDP KIAESICDAA EQFGFFQLVN HGVPLEVLDG VKDATHCFFG LPAEEKRKFS
KELSSTNNVR FGTSFSPDSE KALEWKDYLS LFYVSEDEAS ALWPSACKDE CLEYMKKSEV
LCRKLMTSLM ERLNVKEIDE TKESLLMGSK RINLNYYPRC PNPQLTIGVG RHSDVSSLTF
LLQDEIGGLY VRVNEGKGEE DGWVHVPPVE GSLVINVGDA LQILSNGRYK SVEHCVIASG
SKNRISIPIF VNPKPSDVIG PLPEVLATGE KPKYKNFLYS DYVKHFFRKA HDGKKTVAFA
EI
//
