F6H21_IPOBA
ID F6H21_IPOBA Reviewed; 358 AA.
AC G9M9M4;
DT 05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT 22-FEB-2012, sequence version 1.
DT 03-AUG-2022, entry version 35.
DE RecName: Full=Bi-functional coumaroyl CoA and feruloyl CoA ortho-hydroxylase F6H2-1-1 {ECO:0000303|PubMed:22169019};
DE Short=IbF6H2-1-1 {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 F6H2-1-1 {ECO:0000303|PubMed:22169019};
DE Short=2OGD F6H2-1-1 {ECO:0000303|PubMed:22169019};
GN Name=F6H2-1-1 {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 with 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=14.06 uM for feruloyl-CoA {ECO:0000269|PubMed:22169019};
CC KM=15.25 uM for p-Coumaroyl-CoA {ECO:0000269|PubMed:22169019};
CC Note=kcat is 0.55 sec(-1) with feruloyl-CoA as substrate. kcat is
CC 0.64 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 and, at low levels, in tubers, leaves and petioles.
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; AB636153; BAL22347.1; -; mRNA.
DR AlphaFoldDB; G9M9M4; -.
DR SMR; G9M9M4; -.
DR KEGG; ag:BAL22347; -.
DR BioCyc; MetaCyc:MON-18295; -.
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 F6H2-1-1"
FT /id="PRO_0000447356"
FT DOMAIN 207..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; 40386 MW; B5C75E48A1AAFA16 CRC64;
MPSTTLSTVL SDINEFVVKQ GHGVKGLSEL GLQTLPNQYV HPPEERLSSM DVVSDDSIPV
IDVSNWEDPK VAKLICDAAE KRGFFQIVNH GIPLEMLEKA KAATYRFFRE PAEEKKKYSK
ENCPTSHVRY STSFLPQIEK ALEWKDHLSM FYVSDEEAAQ YWPPSCRDDA LEYLKSCEMV
SRKLLEALMQ GLNVNEIDDA KESLLMGSRR ININYYPKCP NPDLTVGVGR HSDISTLTLL
LQDDIGGLYV RKLEHEAWSH VPPVKGALVI NIGDALQIMS NGRYKSIEHR VLANETNDRI
SVPVFVNPKP NDIVGPLPEV LASGEKPVYK PVLYSDYAKH FYRKAHNGKD TIAFARIE
