ID   F6H11_IPOBA             Reviewed;         358 AA.
AC   G9M9M0;
DT   05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT   22-FEB-2012, sequence version 1.
DT   03-AUG-2022, entry version 31.
DE   RecName: Full=Feruloyl CoA ortho-hydroxylase F6H1-1 {ECO:0000303|PubMed:22169019};
DE            Short=IbF6H1-1 {ECO:0000303|PubMed:22169019};
DE            EC=1.14.11.61 {ECO:0000250|UniProtKB:G9M9M1, ECO:0000255|PROSITE-ProRule:PRU00805};
DE   AltName: Full=2-oxoglutarate-dependent dioxygenase F6H1-1 {ECO:0000303|PubMed:22169019};
DE            Short=2OGD F6H1-1 {ECO:0000303|PubMed:22169019};
GN   Name=F6H1-1 {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], AND FUNCTION.
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 (Probable). Converts feruloyl CoA
CC       into 6'-hydroxyferuloyl CoA (By similarity).
CC       {ECO:0000250|UniProtKB:G9M9M1, ECO:0000305|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:0000250|UniProtKB:G9M9M1};
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   -!- PATHWAY: Phenylpropanoid metabolism. {ECO:0000305|PubMed:22169019}.
CC   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family. {ECO:0000305}.
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DR   EMBL; AB636149; BAL22343.1; -; mRNA.
DR   AlphaFoldDB; G9M9M0; -.
DR   SMR; G9M9M0; -.
DR   GO; GO:0016706; F:2-oxoglutarate-dependent dioxygenase activity; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009805; P:coumarin biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0009699; P:phenylpropanoid biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0002238; P:response to molecule of fungal origin; IEA:UniProt.
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   2: Evidence at transcript level;
KW   Dioxygenase; Iron; Metal-binding; Oxidoreductase.
FT   CHAIN           1..358
FT                   /note="Feruloyl CoA ortho-hydroxylase F6H1-1"
FT                   /id="PRO_0000447353"
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;  39932 MW;  627EBA442EF28F47 CRC64;
     MPAVLSSVLS NITDFVVHEG NGVKGLADMG LEALPKQYVQ PEEERITTST VIVDDTIPVI
     DLSEWGSDPK VGDMNCEAAE KWGFFQIVNH GVPLEVLEEV KAATYRFFRL PAEEKNKHSK
     DNSPSNNVRY GTSFTPHAEK ALEWKDFLSL FYVSDEEAAA LWPSACRDEA LTFMRNCDAV
     IKRLLKSLMK GLNVTEIDGT KESLLMGSKR INMNYYPKCP NPELTVGVGR HSDVSTLTIL
     LQDQIGGLYV RKLDSDEWVH VPPINGAIVI NVGDALQILS NGRYKSIEHR VIANGSNNRI
     SVPIFVNPRP NDVIGPLPEL LESGEKAVYK NVLYSDYVKH FFRKAHDGKE TVDFAKIN