F6H28_IPOBA
ID F6H28_IPOBA Reviewed; 359 AA.
AC G9M9M5;
DT 05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT 22-FEB-2012, sequence version 1.
DT 03-AUG-2022, entry version 32.
DE RecName: Full=Bi-functional coumaroyl CoA and feruloyl CoA ortho-hydroxylase F6H2-1-8 {ECO:0000303|PubMed:22169019};
DE Short=IbF6H2-1-8 {ECO:0000303|PubMed:22169019};
DE EC=1.14.11.61 {ECO:0000255|PROSITE-ProRule:PRU00805, ECO:0000269|PubMed:22169019};
DE EC=1.14.11.62 {ECO:0000255|PROSITE-ProRule:PRU00805, ECO:0000269|PubMed:22169019};
DE AltName: Full=2-oxoglutarate-dependent dioxygenase F6H2-1-8 {ECO:0000303|PubMed:22169019};
DE Short=2OGD F6H2-1-8 {ECO:0000303|PubMed:22169019};
GN Name=F6H2-1-8 {ECO:0000303|PubMed:22169019};
OS Ipomoea batatas (Sweet potato) (Convolvulus batatas).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Convolvulaceae; Ipomoeeae; Ipomoea.
OX NCBI_TaxID=4120;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION BY FUNGAL AND CHITOSAN TREATMENTS,
RP AND TISSUE SPECIFICITY.
RC TISSUE=Root tuber;
RX PubMed=22169019; DOI=10.1016/j.phytochem.2011.11.009;
RA Matsumoto S., Mizutani M., Sakata K., Shimizu B.;
RT "Molecular cloning and functional analysis of the ortho-hydroxylases of p-
RT coumaroyl coenzyme A/feruloyl coenzyme A involved in formation of
RT umbelliferone and scopoletin in sweet potato, Ipomoea batatas (L.) Lam.";
RL Phytochemistry 74:49-57(2012).
CC -!- FUNCTION: 2-oxoglutarate (OG)- and Fe(II)-dependent dioxygenase (2OGD)
CC involved in scopoletin and umbelliferone biosynthesis
CC (PubMed:22169019). Converts feruloyl CoA into 6'-hydroxyferuloyl CoA,
CC and p-coumaroyl CoA into 2,4-dihydroxycinnamoyl-CoA, but has no
CC activity with caffeoyl-CoA (PubMed:22169019).
CC {ECO:0000269|PubMed:22169019}.
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:22169019};
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:22169019};
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7.34 uM for feruloyl-CoA {ECO:0000269|PubMed:22169019};
CC KM=7.92 uM for p-Coumaroyl-CoA {ECO:0000269|PubMed:22169019};
CC Note=kcat is 0.28 sec(-1) with feruloyl-CoA as substrate. kcat is
CC 0.28 sec(-1) with p-Coumaroyl-CoA as substrate.
CC {ECO:0000269|PubMed:22169019};
CC pH dependence:
CC Optimum pH is 7.2. {ECO:0000269|PubMed:22169019};
CC -!- PATHWAY: Phenylpropanoid metabolism. {ECO:0000269|PubMed:22169019}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in underground stems and stems,
CC and, at low levels, in tubers, leaves and petioles.
CC {ECO:0000269|PubMed:22169019}.
CC -!- INDUCTION: Transiently induced by fungal (F.oxysporum f.sp. batatas O-
CC 17) and chitosan treatments, in association with the accumulation of
CC umbelliferone and its glucoside (skimmin) in the tubers.
CC {ECO:0000269|PubMed:22169019}.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; AB636154; BAL22348.1; -; mRNA.
DR AlphaFoldDB; G9M9M5; -.
DR SMR; G9M9M5; -.
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:0009620; P:response to fungus; IEP:UniProtKB.
DR GO; GO:0002238; P:response to molecule of fungal origin; 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..359
FT /note="Bi-functional coumaroyl CoA and feruloyl CoA ortho-
FT hydroxylase F6H2-1-8"
FT /id="PRO_0000447358"
FT DOMAIN 201..309
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 217
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:D4N500"
FT BINDING 232
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 234
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 290
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 300
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 302
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:D4N500"
SQ SEQUENCE 359 AA; 40515 MW; 63E366C49BC37E2B CRC64;
MMPSTTLSTV LSDINEFVVK QGHGVKGLSE LGLQTLPNQY VHPPEERLSS MDVVSDDSIP
VIDVSNWEDP KVAKLICNAA EKRGFFQIVN HGIPLEMLEK AKAATYRFFR EPAQEKKKYS
KENCPTSHVR YSTSFLPQIE KALEWKDHLS MFYVSDQEAA QYWPPSCRDD ALEYLKSCEL
VSRKLLEALM QGLNVNQIDD SKESLLMGSR RININYYPKC PNPDLTVGVG RHSDISTLTL
LLQDDIGGLY VRKLEHEAWS HVPPVKGALV INIGDALQIM SNGRYKSIEH RVMANESNDR
ISVPVFVNPK PNDIVGPLPE VLASGEKPVY KPVLYSDYAK HFYRKAHNGK DTIAFARIE
