ID F6H12_IPOBA Reviewed; 358 AA. AC G9M9M1; DT 05-JUN-2019, integrated into UniProtKB/Swiss-Prot. DT 22-FEB-2012, sequence version 1. DT 31-JUL-2019, entry version 24. DE RecName: Full=Feruloyl CoA ortho-hydroxylase F6H1-2 {ECO:0000303|PubMed:22169019}; DE Short=IbF6H1-2 {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 F6H1-2 {ECO:0000303|PubMed:22169019}; DE Short=2OGD F6H1-2 {ECO:0000303|PubMed:22169019}; GN Name=F6H1-2 {ECO:0000303|PubMed:22169019}; OS Ipomoea batatas (Sweet potato) (Convolvulus batatas). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; OC Pentapetalae; asterids; lamiids; Solanales; Convolvulaceae; Ipomoeeae; OC 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 RT of p-coumaroyl coenzyme A/feruloyl coenzyme A involved in formation of RT umbelliferone and scopoletin in sweet potato, Ipomoea batatas (L.) RT Lam."; RL Phytochemistry 74:49-57(2012). CC -!- FUNCTION: 2-oxoglutarate (OG)- and Fe(II)-dependent dioxygenase CC (2OGD) involved in scopoletin biosynthesis (PubMed:22169019). CC Converts feruloyl CoA into 6'-hydroxyferuloyl CoA, and, at low CC efficiency, caffeoyl-CoA into 6'-hydroxycaffeate, but has no CC activity with p-coumaroyl-CoA (PubMed:22169019). CC {ECO:0000269|PubMed:22169019}. CC -!- CATALYTIC ACTIVITY: CC Reaction=2-oxoglutarate + O2 + trans-feruloyl-CoA = (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=9.15 uM for feruloyl-CoA {ECO:0000269|PubMed:22169019}; CC Note=kcat is 2.68 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. CC {ECO:0000269|PubMed:22169019}. CC -!- TISSUE SPECIFICITY: Expressed at low levels in tubers, underground CC stems, leaves and petioles. {ECO:0000269|PubMed:22169019}. CC -!- INDUCTION: Transiently induced by fungal (F.oxysporum f.sp. CC 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB636150; BAL22344.1; -; mRNA. 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; IPR027443; IPNS-like. 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 Feruloyl CoA ortho-hydroxylase F6H1-2. FT /FTId=PRO_0000447354. FT DOMAIN 200 308 Fe2OG dioxygenase. {ECO:0000255|PROSITE- FT ProRule:PRU00805}. FT METAL 231 231 Iron. {ECO:0000255|PROSITE- FT ProRule:PRU00805}. FT METAL 233 233 Iron. {ECO:0000255|PROSITE- FT ProRule:PRU00805}. FT METAL 289 289 Iron. {ECO:0000255|PROSITE- FT ProRule:PRU00805}. FT BINDING 216 216 2-oxoglutarate. FT {ECO:0000250|UniProtKB:D4N500}. FT BINDING 299 299 2-oxoglutarate. {ECO:0000255|PROSITE- FT ProRule:PRU00805}. FT BINDING 301 301 2-oxoglutarate. FT {ECO:0000250|UniProtKB:D4N500}. SQ SEQUENCE 358 AA; 39934 MW; 20E38C691B87A0FE CRC64; MPAVLSSVLS NITDFVVHEG NGVKGLADMG LEALPKQYVQ PEEERITTST VIVDDTIPVI DLSEWGSDPK VGDMICEAAE KWGFFQIVNH GVPLEVLEEV KAATYRFFRL PAEEKNKHCK DNSPSNNVRY GTSFTPHAEK ALEWKDFLSL FYVSDEEAAA LWPSACRDEA LTFMRNCDAV IKRLLKSLMK GLNVTEIDGT KESLLMGSKR INMNYYPKCP NPELTVGVGR HSDVSTLTIL LQDQIGGLYV RKLDSDTWVH VPPINGAIVI NVGDALQILS NGRYKSIEHR VIANGSNNRI SVPIFVNPRP NDIIGPLPEL LESGEKAVYK NVLYSDYVKH FFRKAHDGKE TVDFAKIN //