DIOX4_RUTGR
ID DIOX4_RUTGR Reviewed; 367 AA.
AC W5QJZ5;
DT 05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 29.
DE RecName: Full=Bi-functional coumaroyl CoA and feruloyl CoA ortho-hydroxylase Diox4 {ECO:0000303|PubMed:22168819};
DE EC=1.14.11.61 {ECO:0000255|PROSITE-ProRule:PRU00805, ECO:0000269|PubMed:22168819};
DE EC=1.14.11.62 {ECO:0000255|PROSITE-ProRule:PRU00805, ECO:0000269|PubMed:22168819};
DE AltName: Full=2-oxoglutarate-dependent dioxygenase 4 {ECO:0000303|PubMed:22168819};
DE Short=2OGD Diox4 {ECO:0000303|PubMed:22168819};
GN Name=DIOX4 {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], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION BY UV-B LIGHT, ACTIVITY
RP REGULATION, AND PATHWAY.
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
CC (PubMed:22168819). Converts feruloyl CoA into 6'-hydroxyferuloyl CoA,
CC and p-coumaroyl CoA into 2,4-dihydroxycinnamoyl-CoA (PubMed:22168819).
CC Has no activity with cinnamic acid, caffeic acid, p-coumaric acid,
CC ferulic acid, cinnamoyl-CoA and caffeoyl-CoA (PubMed:22168819).
CC {ECO:0000269|PubMed:22168819}.
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:0000269|PubMed:22168819};
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:0000269|PubMed:22168819};
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 -!- ACTIVITY REGULATION: Repressed by the competitive inhibitor psoralen,
CC but not by umbelliferone, xanthotoxin, bergapten and isopimpinellin.
CC {ECO:0000269|PubMed:22168819}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=37 uM for feruloyl-CoA {ECO:0000269|PubMed:22168819};
CC KM=50 uM for p-coumaroyl-CoA {ECO:0000269|PubMed:22168819};
CC Note=kcat is 0.46 sec(-1) with feruloyl-CoA as substrate
CC (PubMed:22168819). kcat is 0.71 sec(-1) with p-coumaroyl-CoA as
CC substrate (PubMed:22168819). {ECO:0000269|PubMed:22168819};
CC -!- PATHWAY: Phenylpropanoid metabolism. {ECO:0000269|PubMed:22168819}.
CC -!- INDUCTION: Induced by UV-B in leaves and petioles, but not in roots and
CC stems. {ECO:0000269|PubMed:22168819}.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; GU460158; ADV77970.1; -; mRNA.
DR AlphaFoldDB; W5QJZ5; -.
DR SMR; W5QJZ5; -.
DR BioCyc; MetaCyc:MON-17096; -.
DR GO; GO:0016706; F:2-oxoglutarate-dependent dioxygenase activity; IDA: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; IDA:UniProtKB.
DR GO; GO:0009699; P:phenylpropanoid biosynthetic process; IDA:UniProtKB.
DR GO; GO:0010224; P:response to UV-B; IEP: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 1: Evidence at protein level;
KW Dioxygenase; Iron; Metal-binding; Oxidoreductase.
FT CHAIN 1..367
FT /note="Bi-functional coumaroyl CoA and feruloyl CoA ortho-
FT hydroxylase Diox4"
FT /id="PRO_0000447361"
FT DOMAIN 207..317
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 223
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:D4N500"
FT BINDING 238
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 240
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 298
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 308
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 310
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:D4N500"
SQ SEQUENCE 367 AA; 41821 MW; A7E1121E1D075146 CRC64;
MAPTKDSVIH MGAESWDEIS EFVTKKGHGV KGLSELGIKT LPKQFHQPLE ERFSEKKILE
RASIPLIDMS KWDSPEVVKS ICDAAEHWGF FQIVNHGVPL ETLQRVKEAT HRFFALPAEE
KNKYSKENSP INNVRFGSSF VPHVEKALEW KDFLSMFYVS EEETNTYWPP ICRDEMLEYM
RSSEVLIKRL MEVLVVKGLK VKQIDEIREP MLVGSRRINL NYYPKCPNPE LTLGVGRHSD
ISTFTILLQD EIGGLHVRKL DDTGNTWVHV TPISGSLIIN IGDALQIMSN GRYKSIEHMV
VANGTQDRIS VPLFVNPKPQ AILCPFPEVL ANGEKPVYKP VLCSDYSRHF YTKPHDGKKT
VDFALMN
