DIOX1_RUTGR
ID DIOX1_RUTGR Reviewed; 369 AA.
AC A0A023GS28;
DT 05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT 09-JUL-2014, sequence version 1.
DT 03-AUG-2022, entry version 27.
DE RecName: Full=Bi-functional coumaroyl CoA and feruloyl CoA ortho-hydroxylase Diox1 {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 1 {ECO:0000303|PubMed:22168819};
GN Name=DIOX1 {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; GU460156; ADV77968.1; -; mRNA.
DR AlphaFoldDB; A0A023GS28; -.
DR SMR; A0A023GS28; -.
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 Diox1"
FT /id="PRO_0000447359"
FT DOMAIN 209..319
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 225
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:D4N500"
FT BINDING 240
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 242
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 300
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 310
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 312
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:D4N500"
SQ SEQUENCE 369 AA; 41879 MW; 4278BABF096E48FD CRC64;
MAPTKDFSTT TTNGAESWDD VADFVTKKGH GVKGLSERGI KTLPKPFHQP LEERFSEKKI
LERASIPLID MSQWDSPEVV KSICDAAENW GFFQIVNHGV PLETLERVKE ATHRFFGLPA
EEKNNYSKEN SPINNVRFGS SFVPHVEKAL EWKDFLSMFY VSEEETNTYW PPICRDEMLE
YMRSSEVLIQ RLMEVLVVKG LKVKQIDEIR EPMLVGSRRI NLNYYPKCPN PELTLGVGRH
SDISTFTILL QDQIGGLHVR KLDDTGNTWV HVTPIAGSLI INIGDALQIM SNGRYKSIEH
MVVANGTQDR ISVPLFVNPK PQAILCPFPE VLANGEKPVY KPVFCSDYSR HFYTKPHDGK
KTVDVAMIN
