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 11-DEC-2019, entry version 26. 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; 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=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. {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. 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}. 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 FT /note="Feruloyl CoA ortho-hydroxylase F6H1-2" FT /id="PRO_0000447354" FT DOMAIN 200..308 FT /note="Fe2OG dioxygenase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805" FT METAL 231 FT /note="Iron" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805" FT METAL 233 FT /note="Iron" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805" FT METAL 289 FT /note="Iron" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805" FT BINDING 216 FT /note="2-oxoglutarate" FT /evidence="ECO:0000250|UniProtKB:D4N500" FT BINDING 299 FT /note="2-oxoglutarate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805" FT BINDING 301 FT /note="2-oxoglutarate" FT /evidence="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 //