F6H22_IPOBA
ID F6H22_IPOBA Reviewed; 358 AA.
AC G9M9M3;
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 F6H2-2-1 {ECO:0000303|PubMed:22169019};
DE Short=IbF6H2-2-1 {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 F6H2-2-1 {ECO:0000303|PubMed:22169019};
DE Short=2OGD F6H2-2-1 {ECO:0000303|PubMed:22169019};
GN Name=F6H2-2-1 {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], 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 toward 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=7.46 uM for feruloyl-CoA {ECO:0000269|PubMed:22169019};
CC KM=6.12 uM for p-Coumaroyl-CoA {ECO:0000269|PubMed:22169019};
CC Note=kcat is 0.35 sec(-1) with feruloyl-CoA as substrate. kcat is
CC 0.33 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 {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; AB636152; BAL22346.1; -; mRNA.
DR AlphaFoldDB; G9M9M3; -.
DR SMR; G9M9M3; -.
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..358
FT /note="Bi-functional coumaroyl CoA and feruloyl CoA ortho-
FT hydroxylase F6H2-2-1"
FT /id="PRO_0000447357"
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; 40405 MW; 7B72A5CC0E7CF223 CRC64;
MPSTTLSTVL SDINDFVVKQ GHGVKGLSEL GLQTLPNQYV HPPEERLSSM DVVSDDSIPV
IDVSNWEDPK VAKLICDAAE KRGFFQIVNH GIPIEMLEKA KAATYRFFRE PAEEKKKYSK
ENCPTSHVRY STSFLPQIEK ALEWKDHLSM FYVSDEEAAQ YWPPSCRDDA VEYLKSCEMV
SRKLLEALMQ GLNVNQIDDS KESLLMGSRR ININYYPKCP NPDLTVGVGR HSDISTLTLL
LQDDIGGLYV RKLEHEAWSH VPPVKGALVI NIGDALQIMS NGRYKSIEHR VMANESNDRI
SVPVFVNPRP NDIVGPLPEV LASGEKPVYK PVLYSDYAKH FYRKAHNGKD TIAFARIE
