S8H_ARATH
ID S8H_ARATH Reviewed; 357 AA.
AC Q9LE86; A0A178VF14; A0MEV7;
DT 16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Scopoletin 8-hydroxylase {ECO:0000303|PubMed:29581584};
DE EC=1.14.11.60 {ECO:0000255|PROSITE-ProRule:PRU00805, ECO:0000269|PubMed:29581584};
DE AltName: Full=2-oxoglutarate-dependent dioxygenase S8H {ECO:0000305|PubMed:29581584};
GN Name=S8H {ECO:0000303|PubMed:29581584};
GN OrderedLocusNames=At3g12900 {ECO:0000312|Araport:AT3G12900};
GN ORFNames=MJM20.4 {ECO:0000312|EMBL:AAF34829.1};
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, INDUCTION BY
RP IRON-DEFICIENCY, PATHWAY, AND TISSUE SPECIFICITY.
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).
CC -!- FUNCTION: Involved in the pathway of sideretin biosynthesis from
CC feruloyl CoA, a redox-active catecholic metabolite exuded by roots in
CC response to iron deficiency in order to facilitate the uptake of iron;
CC this pathway consists in the successive conversion from feruloyl CoA to
CC scopoletin, from scopoletin to fraxetin and from fraxetin to sideretin.
CC Catalyzes the biosynthesis of fraxetin via scopoletin hydroxylation.
CC {ECO:0000269|PubMed:29581584}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + O2 + scopoletin = CO2 + fraxetin + succinate;
CC Xref=Rhea:RHEA:57848, ChEBI:CHEBI:5169, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:17488,
CC ChEBI:CHEBI:30031; EC=1.14.11.60;
CC Evidence={ECO:0000269|PubMed:29581584};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57849;
CC Evidence={ECO:0000269|PubMed:29581584};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000250|UniProtKB:Q9LHN8};
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:0000269|PubMed:29581584}.
CC -!- TISSUE SPECIFICITY: Expressed in both primary and lateral roots under
CC iron-deficient conditions, except in apical root zones, and mostly in
CC the root epidermal layer. {ECO:0000269|PubMed:29581584}.
CC -!- INDUCTION: Strongly induced by iron deficiency, mainly in roots.
CC {ECO:0000269|PubMed:29581584}.
CC -!- DISRUPTION PHENOTYPE: Accumulation of scopoletin, but loss of sideretin
CC root secretion in response to iron deficiency. Impaired iron-uptake
CC ability at elevated pH leading to chlorotic and stunted plants; this
CC phenotype is rescued by fraxetin and sideretin treatments, but not by
CC scopoletin treatment. {ECO:0000269|PubMed:29581584}.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABK28555.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AP000385; BAB01419.1; -; Genomic_DNA.
DR EMBL; AC023838; AAF34829.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75258.1; -; Genomic_DNA.
DR EMBL; DQ446658; ABE65937.1; -; mRNA.
DR EMBL; DQ653080; ABK28555.1; ALT_SEQ; mRNA.
DR RefSeq; NP_187896.1; NM_112126.2.
DR AlphaFoldDB; Q9LE86; -.
DR SMR; Q9LE86; -.
DR STRING; 3702.AT3G12900.1; -.
DR PaxDb; Q9LE86; -.
DR PRIDE; Q9LE86; -.
DR ProteomicsDB; 189217; -.
DR EnsemblPlants; AT3G12900.1; AT3G12900.1; AT3G12900.
DR GeneID; 820473; -.
DR Gramene; AT3G12900.1; AT3G12900.1; AT3G12900.
DR KEGG; ath:AT3G12900; -.
DR Araport; AT3G12900; -.
DR TAIR; locus:2090359; AT3G12900.
DR eggNOG; KOG0143; Eukaryota.
DR HOGENOM; CLU_010119_16_4_1; -.
DR InParanoid; Q9LE86; -.
DR OMA; WPNQCKE; -.
DR OrthoDB; 622449at2759; -.
DR PhylomeDB; Q9LE86; -.
DR BioCyc; ARA:AT3G12900-MON; -.
DR BioCyc; MetaCyc:AT3G12900-MON; -.
DR BRENDA; 1.14.11.60; 399.
DR PRO; PR:Q9LE86; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LE86; baseline and differential.
DR GO; GO:0016706; F:2-oxoglutarate-dependent dioxygenase activity; IDA:TAIR.
DR GO; GO:0051213; F:dioxygenase activity; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0106145; F:scopoletin 8-hydroxylase activity; IDA:TAIR.
DR GO; GO:0009805; P:coumarin biosynthetic process; IDA:TAIR.
DR GO; GO:0106147; P:fraxetin biosynthesis; IDA:TAIR.
DR GO; GO:0010039; P:response to iron ion; IEP:TAIR.
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..357
FT /note="Scopoletin 8-hydroxylase"
FT /id="PRO_0000446019"
FT DOMAIN 206..307
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 288
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 298
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 300
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:D4N500"
SQ SEQUENCE 357 AA; 39716 MW; 06576D8EC827AD67 CRC64;
MGINFEDQTT LFNFVVREGN GVKGMIDSGL SSVPRPFVQP LSERIPTQKA LTCEATQPID
LSNLDGPQHK EVAKQIVEAA ETLGFFQVVN HGVSVELLEL LKSSAHEFFA QAPEEKSMYL
KEVSPSKLVK YGTSFVPDKE KAIEWKDYVS MLYTNDSEAL QHWPQPCREV ALEFLNSSME
MVKNVVNILM ENVGVTLEEE KMNGLMGTKM VNMNYYPTCP SPELTVGVGR HSDMGMLTVL
LQDGIGGLYV KLDNGEWAEI PPVHGALVIN IGDTLQILSN GKYKSAEHRV RTTNIGSRVS
VPIFTAPNPS QKVGPLPEVV KRDGVARYKE FLFQDYMNNF FGQPHDGKKS LDFARAE
