F6H2_ARATH
ID F6H2_ARATH Reviewed; 361 AA.
AC Q9C899;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Feruloyl CoA ortho-hydroxylase 2 {ECO:0000303|PubMed:18547395};
DE EC=1.14.11.61 {ECO:0000269|PubMed:18547395};
GN Name=F6'H2 {ECO:0000303|PubMed:18547395};
GN OrderedLocusNames=At1g55290 {ECO:0000312|Araport:AT1G55290};
GN ORFNames=F7A10.24 {ECO:0000312|EMBL:AAG51560.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 Kim C.J., Chen H., Cheuk R., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
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).
CC -!- FUNCTION: 2-oxoglutarate (OG)- and Fe(II)-dependent dioxygenase
CC (2OGD)involved in scopoletin biosynthesis. Converts feruloyl CoA into
CC 6'-hydroxyferuloyl CoA but has no activity with ferulic acid,
CC feruloylquinic acid, caffeic acid, caffeoyl CoA, p-coumaric acid,
CC cinnamic acid, cinnamoyl CoA or benzoyl CoA.
CC {ECO:0000269|PubMed:18547395}.
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 -!- 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=14.5 uM for feruloyl CoA {ECO:0000269|PubMed:18547395};
CC Note=kcat is 4.79 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 -!- TISSUE SPECIFICITY: Low expression in roots.
CC {ECO:0000269|PubMed:18547395}.
CC -!- INDUCTION: Not induced by 2,4-D treatment.
CC {ECO:0000269|PubMed:18547395}.
CC -!- DISRUPTION PHENOTYPE: No effect on scopoletin and scopolin levels in
CC the roots. {ECO:0000269|PubMed:18547395}.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; AC027034; AAG51560.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33219.1; -; Genomic_DNA.
DR EMBL; BT011228; AAR92264.1; -; mRNA.
DR EMBL; BT012156; AAS76251.1; -; mRNA.
DR PIR; H96594; H96594.
DR RefSeq; NP_175925.1; NM_104404.4.
DR AlphaFoldDB; Q9C899; -.
DR SMR; Q9C899; -.
DR BioGRID; 27199; 1.
DR IntAct; Q9C899; 1.
DR STRING; 3702.AT1G55290.1; -.
DR PaxDb; Q9C899; -.
DR PRIDE; Q9C899; -.
DR ProteomicsDB; 222259; -.
DR EnsemblPlants; AT1G55290.1; AT1G55290.1; AT1G55290.
DR GeneID; 841974; -.
DR Gramene; AT1G55290.1; AT1G55290.1; AT1G55290.
DR KEGG; ath:AT1G55290; -.
DR Araport; AT1G55290; -.
DR TAIR; locus:2035671; AT1G55290.
DR eggNOG; KOG0143; Eukaryota.
DR HOGENOM; CLU_010119_16_4_1; -.
DR OMA; QAHDSIP; -.
DR OrthoDB; 755305at2759; -.
DR PhylomeDB; Q9C899; -.
DR BioCyc; ARA:AT1G55290-MON; -.
DR PRO; PR:Q9C899; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C899; baseline and differential.
DR Genevisible; Q9C899; AT.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; Reference proteome.
FT CHAIN 1..361
FT /note="Feruloyl CoA ortho-hydroxylase 2"
FT /id="PRO_0000419519"
FT DOMAIN 211..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"
SQ SEQUENCE 361 AA; 40876 MW; 911C8E76D9DCD07A CRC64;
MNQTLAAQFL TRDQVTNFVV HEGNGVKGLS ETGIKVLPDQ YIQPFEERLI NFHVKEDSDE
SIPVIDISNL DEKSVSKAVC DAAEEWGFFQ VINHGVSMEV LENMKTATHR FFGLPVEEKR
KFSREKSLST NVRFGTSFSP HAEKALEWKD YLSLFFVSEA EASQLWPDSC RSETLEYMNE
TKPLVKKLLR FLGENLNVKE LDKTKESFFM GSTRINLNYY PICPNPELTV GVGRHSDVSS
LTILLQDEIG GLHVRSLTTG RWVHVPPISG SLVINIGDAM QIMSNGRYKS VEHRVLANGS
YNRISVPIFV SPKPESVIGP LLEVIENGEK PVYKDILYTD YVKHFFRKAH DGKKTIDFAN
I
