F6H13_IPOBA
ID F6H13_IPOBA Reviewed; 358 AA.
AC G9M9M2;
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=Feruloyl CoA ortho-hydroxylase F6H1-3 {ECO:0000303|PubMed:22169019};
DE Short=IbF6H1-3 {ECO:0000303|PubMed:22169019};
DE EC=1.14.11.61 {ECO:0000255|PROSITE-ProRule:PRU00805, ECO:0000269|PubMed:22169019};
DE AltName: Full=2-oxoglutarate-dependent dioxygenase F6H1-3 {ECO:0000303|PubMed:22169019};
DE Short=2OGD F6H1-3 {ECO:0000303|PubMed:22169019};
GN Name=F6H1-3 {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, 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 biosynthesis (PubMed:22169019). Converts
CC feruloyl CoA into 6'-hydroxyferuloyl CoA, and, at low efficiency,
CC caffeoyl-CoA into 6'-hydroxycaffeate, but has no activity with p-
CC coumaroyl-CoA (PubMed:22169019). {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=10.15 uM for feruloyl-CoA {ECO:0000269|PubMed:22169019};
CC Note=kcat is 2.84 sec(-1) with feruloyl-CoA as substrate.
CC {ECO:0000269|PubMed:22169019};
CC pH dependence:
CC Optimum pH is 6.5. {ECO:0000269|PubMed:22169019};
CC -!- PATHWAY: Phenylpropanoid metabolism. {ECO:0000269|PubMed:22169019}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in tubers, and, at low levels, in
CC underground stems, stems, leaves and petioles.
CC {ECO:0000269|PubMed:22169019}.
CC -!- INDUCTION: Transiently induced at low levels by fungal (F.oxysporum
CC f.sp. batatas O-17) and chitosan treatments, in association with the
CC accumulation of umbelliferone and its glucoside (skimmin) in the
CC tubers. {ECO:0000269|PubMed:22169019}.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; AB636151; BAL22345.1; -; mRNA.
DR AlphaFoldDB; G9M9M2; -.
DR SMR; G9M9M2; -.
DR BRENDA; 1.14.11.61; 2773.
DR GO; GO:0016706; F:2-oxoglutarate-dependent dioxygenase activity; IDA:UniProtKB.
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..358
FT /note="Feruloyl CoA ortho-hydroxylase F6H1-3"
FT /id="PRO_0000447355"
FT DOMAIN 200..308
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 216
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:D4N500"
FT BINDING 231
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 233
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 289
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 299
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 301
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:D4N500"
SQ SEQUENCE 358 AA; 39871 MW; CB3E1F8D8C214945 CRC64;
MPAVLSSVLS NITDFVVHEG NGVKGLADMG LQSLPKQYIQ PAEERITTST VIVDDTIPVI
DLSEWGSDPK VGDLICEAAE KWGFFQIVNH GVPLEVLEEV KAATYRFFRL PAEEKNKHSK
DNSPSNNVRY GTSFTPHAEK ALEWKDFLSL FYVSDEEAAA LWPSACRDEA LTFMRNCDAV
IKRLLKSLMK GLNVTEIDGT KESLLMGSKR INMNYYPKCP NPELTVGVGR HSDVSTLTIL
LQDQIGGLYV RKLDSDTWVH VPPINGAIVI NVGDALQILS NGRYKSIEHR VIANGSNNRI
SVPIFVNPRP NDIIGPLPEL LESGEKAVYK NVLYSDYVKH FFRKAHDGKE TVDFAKIN
