F6H1_ARATH
ID F6H1_ARATH Reviewed; 361 AA.
AC Q9LHN8;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Feruloyl CoA ortho-hydroxylase 1 {ECO:0000303|PubMed:18547395};
DE EC=1.14.11.61 {ECO:0000269|PubMed:18547395, ECO:0000269|PubMed:29581584};
GN Name=F6'H1 {ECO:0000303|PubMed:18547395};
GN OrderedLocusNames=At3g13610 {ECO:0000312|Araport:AT3G13610};
GN ORFNames=K20M4.5 {ECO:0000312|EMBL:BAB02603.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Cheuk R., Chen H., Kim C.J., Shinn P., Carninci P., Hayashizaki Y.,
RA Ishida J., Kamiya A., Kawai J., Narusaka M., Sakurai T., Satou M., Seki M.,
RA Shinozaki K., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, TISSUE SPECIFICITY, DISRUPTION
RP PHENOTYPE, INDUCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=18547395; DOI=10.1111/j.1365-313x.2008.03568.x;
RA Kai K., Mizutani M., Kawamura N., Yamamoto R., Tamai M., Yamaguchi H.,
RA Sakata K., Shimizu B.;
RT "Scopoletin is biosynthesized via ortho-hydroxylation of feruloyl CoA by a
RT 2-oxoglutarate-dependent dioxygenase in Arabidopsis thaliana.";
RL Plant J. 55:989-999(2008).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION BY IRON-DEFICIENCY.
RC STRAIN=cv. Columbia;
RX PubMed=23735511; DOI=10.1104/pp.113.220426;
RA Rodriguez-Celma J., Lin W.-D., Fu G.-M., Abadia J., Lopez-Millan A.-F.,
RA Schmidt W.;
RT "Mutually exclusive alterations in secondary metabolism are critical for
RT the uptake of insoluble iron compounds by Arabidopsis and Medicago
RT truncatula.";
RL Plant Physiol. 162:1473-1485(2013).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND INDUCTION BY
RP IRON-DEFICIENCY.
RC STRAIN=cv. Columbia;
RX PubMed=24246380; DOI=10.1104/pp.113.228544;
RA Schmid N.B., Giehl R.F.H., Doell S., Mock H.-P., Strehmel N., Scheel D.,
RA Kong X., Hider R.C., von Wiren N.;
RT "Feruloyl-CoA 6'-Hydroxylase1-dependent coumarins mediate iron acquisition
RT from alkaline substrates in Arabidopsis.";
RL Plant Physiol. 164:160-172(2014).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=cv. Columbia;
RX PubMed=29581584; DOI=10.1038/s41589-018-0019-2;
RA Rajniak J., Giehl R.F.H., Chang E., Murgia I., von Wiren N., Sattely E.S.;
RT "Biosynthesis of redox-active metabolites in response to iron deficiency in
RT plants.";
RL Nat. Chem. Biol. 14:442-450(2018).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.77 ANGSTROMS) OF 2-361.
RX PubMed=25993561; DOI=10.1038/srep10355;
RA Sun X., Zhou D., Kandavelu P., Zhang H., Yuan Q., Wang B.C., Rose J.,
RA Yan Y.;
RT "Structural insights into substrate specificity of feruloyl-CoA 6'-
RT hydroxylase from Arabidopsis thaliana.";
RL Sci. Rep. 5:10355-10355(2015).
CC -!- FUNCTION: 2-oxoglutarate (OG)- and Fe(II)-dependent dioxygenase (2OGD)
CC involved in scopoletin biosynthesis (PubMed:18547395, PubMed:29581584).
CC Converts feruloyl CoA into 6'-hydroxyferuloyl CoA but has no activity
CC with ferulic acid, feruloylquinic acid, caffeic acid, caffeoyl CoA, p-
CC coumaric acid, cinnamic acid, cinnamoyl CoA or benzoyl CoA
CC (PubMed:18547395). Required for the production and secretion of
CC compounds (e.g. fluorescent coumarins) that facilitate the mobilization
CC and uptake of iron from sources with low bioavailability or in high pH-
CC induced iron deficiency conditions (PubMed:23735511, PubMed:24246380).
CC Involved in the pathway of sideretin biosynthesis from feruloyl CoA, a
CC redox-active catecholic metabolite exuded by roots in response to iron
CC deficiency in order to facilitate the uptake of iron; this pathway
CC consists in the successive conversion from feruloyl CoA to scopoletin,
CC from scopoletin to fraxetin and from fraxetin to sideretin
CC (PubMed:29581584). Catalyzes the biosynthesis of scopoletin from
CC feruloyl CoA (PubMed:29581584). {ECO:0000269|PubMed:18547395,
CC ECO:0000269|PubMed:23735511, ECO:0000269|PubMed:24246380,
CC ECO:0000269|PubMed:29581584}.
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:18547395};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-6-hydroxyferuloyl-CoA = CoA + scopoletin;
CC Xref=Rhea:RHEA:57860, ChEBI:CHEBI:17488, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:142390; Evidence={ECO:0000269|PubMed:18547395,
CC ECO:0000269|PubMed:29581584};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57861;
CC Evidence={ECO:0000269|PubMed:18547395, ECO:0000269|PubMed:29581584};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000269|PubMed:18547395};
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=36 uM for feruloyl CoA {ECO:0000269|PubMed:18547395};
CC Note=kcat is 11 sec(-1) with feruloyl CoA as substrate.
CC {ECO:0000269|PubMed:18547395};
CC pH dependence:
CC Optimum pH is 6.5. {ECO:0000269|PubMed:18547395};
CC -!- PATHWAY: Phenylpropanoid metabolism. {ECO:0000269|PubMed:29581584}.
CC -!- TISSUE SPECIFICITY: Highly expressed in roots, especially in the
CC cortex. {ECO:0000269|PubMed:18547395, ECO:0000269|PubMed:24246380}.
CC -!- INDUCTION: Up-regulated by 2,4-D treatment (PubMed:18547395). Induced
CC by iron deficiency, mainly in roots (PubMed:24246380, PubMed:23735511).
CC {ECO:0000269|PubMed:18547395, ECO:0000269|PubMed:23735511,
CC ECO:0000269|PubMed:24246380}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype, but severe reductions in
CC scopoletin and scopolin levels in the roots (PubMed:18547395,
CC PubMed:29581584). Compromised iron uptake from an iron source of low
CC bioavailability; this phenotype is partially rescued when grown
CC alongside wild-type seedlings, presumably by secreted phenolics and
CC flavins (PubMed:23735511). Loss of fluorescent coumarins (including
CC sideretin, scopolin, scopoletin, esculin, esculetin, and fraxetin) root
CC secretion in response to iron deficiency. Impaired iron-uptake ability
CC at elevated pH (e.g. pH 7.2) leading to chlorotic and stunted plants;
CC this phenotype is rescued by fraxetin, scopoletin, esculin, esculetin
CC and sideretin treatments (PubMed:29581584, PubMed:24246380).
CC {ECO:0000269|PubMed:18547395, ECO:0000269|PubMed:23735511,
CC ECO:0000269|PubMed:24246380, ECO:0000269|PubMed:29581584}.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; AP002038; BAB02603.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75382.1; -; Genomic_DNA.
DR EMBL; BT011745; AAS49108.1; -; mRNA.
DR EMBL; AK221576; BAD95049.1; -; mRNA.
DR RefSeq; NP_187970.1; NM_112207.4.
DR PDB; 4XAE; X-ray; 2.77 A; A/B=2-361.
DR PDBsum; 4XAE; -.
DR AlphaFoldDB; Q9LHN8; -.
DR SMR; Q9LHN8; -.
DR STRING; 3702.AT3G13610.1; -.
DR PaxDb; Q9LHN8; -.
DR PRIDE; Q9LHN8; -.
DR ProteomicsDB; 222258; -.
DR EnsemblPlants; AT3G13610.1; AT3G13610.1; AT3G13610.
DR GeneID; 820564; -.
DR Gramene; AT3G13610.1; AT3G13610.1; AT3G13610.
DR KEGG; ath:AT3G13610; -.
DR Araport; AT3G13610; -.
DR TAIR; locus:2086789; AT3G13610.
DR eggNOG; KOG0143; Eukaryota.
DR HOGENOM; CLU_010119_16_4_1; -.
DR OMA; QNFEKRT; -.
DR OrthoDB; 755305at2759; -.
DR PhylomeDB; Q9LHN8; -.
DR BioCyc; ARA:AT3G13610-MON; -.
DR BioCyc; MetaCyc:AT3G13610-MON; -.
DR BRENDA; 1.14.11.61; 399.
DR PRO; PR:Q9LHN8; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LHN8; baseline and differential.
DR Genevisible; Q9LHN8; AT.
DR GO; GO:0051213; F:dioxygenase activity; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009805; P:coumarin biosynthetic process; IMP:UniProtKB.
DR GO; GO:0010421; P:hydrogen peroxide-mediated programmed cell death; IMP:TAIR.
DR GO; GO:0009699; P:phenylpropanoid biosynthetic process; IMP:TAIR.
DR GO; GO:1990641; P:response to iron ion starvation; IMP: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 3D-structure; Dioxygenase; Iron; Metal-binding; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..361
FT /note="Feruloyl CoA ortho-hydroxylase 1"
FT /id="PRO_0000419518"
FT DOMAIN 204..312
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 220
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:D4N500"
FT BINDING 235
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 237
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 293
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 303
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 305
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:D4N500"
FT HELIX 17..20
FT /evidence="ECO:0007829|PDB:4XAE"
FT TURN 21..23
FT /evidence="ECO:0007829|PDB:4XAE"
FT HELIX 26..31
FT /evidence="ECO:0007829|PDB:4XAE"
FT TURN 32..34
FT /evidence="ECO:0007829|PDB:4XAE"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:4XAE"
FT HELIX 46..52
FT /evidence="ECO:0007829|PDB:4XAE"
FT HELIX 72..85
FT /evidence="ECO:0007829|PDB:4XAE"
FT STRAND 89..93
FT /evidence="ECO:0007829|PDB:4XAE"
FT HELIX 98..112
FT /evidence="ECO:0007829|PDB:4XAE"
FT HELIX 116..119
FT /evidence="ECO:0007829|PDB:4XAE"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:4XAE"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:4XAE"
FT STRAND 132..137
FT /evidence="ECO:0007829|PDB:4XAE"
FT STRAND 140..143
FT /evidence="ECO:0007829|PDB:4XAE"
FT STRAND 150..155
FT /evidence="ECO:0007829|PDB:4XAE"
FT HELIX 160..165
FT /evidence="ECO:0007829|PDB:4XAE"
FT HELIX 171..192
FT /evidence="ECO:0007829|PDB:4XAE"
FT TURN 193..197
FT /evidence="ECO:0007829|PDB:4XAE"
FT HELIX 205..209
FT /evidence="ECO:0007829|PDB:4XAE"
FT STRAND 210..220
FT /evidence="ECO:0007829|PDB:4XAE"
FT TURN 226..228
FT /evidence="ECO:0007829|PDB:4XAE"
FT STRAND 231..235
FT /evidence="ECO:0007829|PDB:4XAE"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:4XAE"
FT STRAND 244..246
FT /evidence="ECO:0007829|PDB:4XAE"
FT STRAND 252..255
FT /evidence="ECO:0007829|PDB:4XAE"
FT STRAND 257..259
FT /evidence="ECO:0007829|PDB:4XAE"
FT STRAND 262..265
FT /evidence="ECO:0007829|PDB:4XAE"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:4XAE"
FT HELIX 278..283
FT /evidence="ECO:0007829|PDB:4XAE"
FT TURN 284..286
FT /evidence="ECO:0007829|PDB:4XAE"
FT STRAND 293..295
FT /evidence="ECO:0007829|PDB:4XAE"
FT STRAND 303..311
FT /evidence="ECO:0007829|PDB:4XAE"
FT HELIX 322..325
FT /evidence="ECO:0007829|PDB:4XAE"
FT HELIX 338..342
FT /evidence="ECO:0007829|PDB:4XAE"
SQ SEQUENCE 361 AA; 40671 MW; 4501ED1E8AA89C82 CRC64;
MAPTLLTTQF SNPAEVTDFV VYKGNGVKGL SETGIKALPE QYIQPLEERL INKFVNETDE
AIPVIDMSNP DEDRVAEAVC DAAEKWGFFQ VINHGVPLEV LDDVKAATHK FFNLPVEEKR
KFTKENSLST TVRFGTSFSP LAEQALEWKD YLSLFFVSEA EAEQFWPDIC RNETLEYINK
SKKMVRRLLE YLGKNLNVKE LDETKESLFM GSIRVNLNYY PICPNPDLTV GVGRHSDVSS
LTILLQDQIG GLHVRSLASG NWVHVPPVAG SFVINIGDAM QIMSNGLYKS VEHRVLANGY
NNRISVPIFV NPKPESVIGP LPEVIANGEE PIYRDVLYSD YVKYFFRKAH DGKKTVDYAK
I
