DIOX2_RUTGR
ID DIOX2_RUTGR Reviewed; 369 AA.
AC A0A023GS29;
DT 05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT 09-JUL-2014, sequence version 1.
DT 03-AUG-2022, entry version 25.
DE RecName: Full=Bi-functional coumaroyl CoA and feruloyl CoA ortho-hydroxylase Diox2 {ECO:0000303|PubMed:22168819};
DE EC=1.14.11.61 {ECO:0000250|UniProtKB:W5QJZ5, ECO:0000255|PROSITE-ProRule:PRU00805};
DE EC=1.14.11.62 {ECO:0000250|UniProtKB:W5QJZ5, ECO:0000255|PROSITE-ProRule:PRU00805};
DE AltName: Full=2-oxoglutarate-dependent dioxygenase 2 {ECO:0000303|PubMed:22168819};
GN Name=DIOX2 {ECO:0000303|PubMed:22168819};
OS Ruta graveolens (Common rue).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Sapindales; Rutaceae; Rutoideae; Ruta.
OX NCBI_TaxID=37565;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=22168819; DOI=10.1111/j.1365-313x.2011.04879.x;
RA Vialart G., Hehn A., Olry A., Ito K., Krieger C., Larbat R., Paris C.,
RA Shimizu B., Sugimoto Y., Mizutani M., Bourgaud F.;
RT "A 2-oxoglutarate-dependent dioxygenase from Ruta graveolens L. exhibits p-
RT coumaroyl CoA 2'-hydroxylase activity (C2'H): a missing step in the
RT synthesis of umbelliferone in plants.";
RL Plant J. 70:460-470(2012).
CC -!- FUNCTION: 2-oxoglutarate (OG)- and Fe(II)-dependent dioxygenase (2OGD)
CC involved in scopoletin and umbelliferone biosynthesis (By similarity).
CC Converts feruloyl CoA into 6'-hydroxyferuloyl CoA, and p-coumaroyl CoA
CC into 2,4-dihydroxycinnamoyl-CoA (By similarity).
CC {ECO:0000250|UniProtKB:W5QJZ5}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-4-coumaroyl-CoA + 2-oxoglutarate + O2 = (E)-2,4-
CC dihydroxycinnamoyl-CoA + CO2 + succinate; Xref=Rhea:RHEA:57868,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:85008, ChEBI:CHEBI:142398;
CC EC=1.14.11.62; Evidence={ECO:0000250|UniProtKB:W5QJZ5};
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:0000250|UniProtKB:W5QJZ5};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000250|UniProtKB:Q9C899};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00805};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00805};
CC -!- PATHWAY: Phenylpropanoid metabolism. {ECO:0000250|UniProtKB:W5QJZ5}.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; GU460157; ADV77969.1; -; mRNA.
DR GO; GO:0016706; F:2-oxoglutarate-dependent dioxygenase activity; ISS:UniProtKB.
DR GO; GO:0102312; F:4-coumaroyl 2'-hydroxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009805; P:coumarin biosynthetic process; ISS:UniProtKB.
DR GO; GO:0009699; P:phenylpropanoid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0010224; P:response to UV-B; ISS:UniProtKB.
DR Gene3D; 2.60.120.330; -; 1.
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 Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR Pfam; PF14226; DIOX_N; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 2: Evidence at transcript level;
KW Dioxygenase; Iron; Metal-binding; Oxidoreductase.
FT CHAIN 1..369
FT /note="Bi-functional coumaroyl CoA and feruloyl CoA ortho-
FT hydroxylase Diox2"
FT /id="PRO_0000447360"
FT DOMAIN 215..318
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 224
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:D4N500"
FT BINDING 239
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 241
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 299
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 309
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 311
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:D4N500"
SQ SEQUENCE 369 AA; 42052 MW; 75B7B7E59C703DC3 CRC64;
MAPTKDFSTA TNGADSWDDV ADFVTKKGHG VKGLSERGIK TLPKPFHQPL EERFSEKKIL
ERASIPLIDM SEWDSPEVVK SICDAAENWG FFQIVNHGVP LETLERVKEA THRFFGLPAE
EKNKYSKENS PINNVRFGSS FVPHVEKALE WKDFLSMFYV SXEETNTYWP PICXDQMLEY
MRSSEVLIKR LMEVLVVKGL KVKQIDEIRE PMLVGSRRVN LNYYPKCPNR ELTLGVGRHS
DISTFTILLQ DQIEVLHVRK LDDTGNTWVH VTPIAGSLII NIGDALQIMS NGRYKSIEHM
VVANGTQDRI SVPLFVNPKP QAILCPFPEV LANGEKPLYK PVFCSDYSRH FYTKPHDGKK
TVDFALINY
