IDS3_HORVU
ID IDS3_HORVU Reviewed; 339 AA.
AC Q40062; Q40063; Q9LU11;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 3.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=2'-deoxymugineic-acid 2'-dioxygenase {ECO:0000303|PubMed:11346963};
DE EC=1.14.11.24 {ECO:0000269|PubMed:11346963};
DE AltName: Full=Protein iron deficiency-specific 3 {ECO:0000303|PubMed:11117263, ECO:0000303|PubMed:8019781};
GN Name=IDS3 {ECO:0000303|PubMed:11117263, ECO:0000303|PubMed:8019781};
OS Hordeum vulgare (Barley).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX NCBI_TaxID=4513;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RC STRAIN=cv. Ehimehadaka No.1; TISSUE=Root;
RX PubMed=8019781;
RA Nakanishi H., Okumura N., Umehara Y., Nishizawa N.-K., Chino M., Mori S.;
RT "Expression of a gene specific for iron deficiency (Ids3) in the roots of
RT Hordeum vulgare.";
RL Plant Cell Physiol. 34:401-410(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, AND INDUCTION BY IRON
RP DEFICIENCY.
RC STRAIN=cv. Igri, and cv. NK 1558; TISSUE=Root;
RX PubMed=11117263; DOI=10.1023/a:1006491521586;
RA Nakanishi H., Yamaguchi H., Sasakuma T., Nishizawa N.K., Mori S.;
RT "Two dioxygenase genes, Ids3 and Ids2, from Hordeum vulgare are involved in
RT the biosynthesis of mugineic acid family phytosiderophores.";
RL Plant Mol. Biol. 44:199-207(2000).
RN [3]
RP PROTEIN SEQUENCE OF 2-12; 80-97 AND 172-191, AND INDUCTION.
RX PubMed=9489019; DOI=10.1104/pp.116.2.725;
RA Suzuki K., Itai R., Suzuki K., Nakanishi H., Nishizawa N.K., Yoshimura E.,
RA Mori S.;
RT "Formate dehydrogenase, an enzyme of anaerobic metabolism, is induced by
RT iron deficiency in barley roots.";
RL Plant Physiol. 116:725-732(1998).
RN [4]
RP FUNCTION, INDUCTION, AND CATALYTIC ACTIVITY.
RX PubMed=11346963; DOI=10.1007/s004250000453;
RA Kobayashi T., Nakanishi H., Takahashi M., Kawasaki S., Nishizawa N.-K.,
RA Mori S.;
RT "In vivo evidence that Ids3 from Hordeum vulgare encodes a dioxygenase that
RT converts 2'-deoxymugineic acid to mugineic acid in transgenic rice.";
RL Planta 212:864-871(2001).
RN [5]
RP FUNCTION.
RX PubMed=17478636; DOI=10.1104/pp.107.096388;
RA Patterson J., Ford K., Cassin A., Natera S., Bacic A.;
RT "Increased abundance of proteins involved in phytosiderophore production in
RT boron-tolerant barley.";
RL Plant Physiol. 144:1612-1631(2007).
CC -!- FUNCTION: Involved in the biosynthesis of mugineic acid family of
CC phytosiderophores. Hydroxylates the C-2' positions of 2'-deoxymugineic
CC acid (DMA) and 3-epihydroxymugineic acid (epiHDMA). May be involved in
CC boron tolerance. {ECO:0000269|PubMed:11117263,
CC ECO:0000269|PubMed:11346963, ECO:0000269|PubMed:17478636}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2'-deoxymugineate + 2-oxoglutarate + O2 = CO2 + mugineate +
CC succinate; Xref=Rhea:RHEA:12200, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:58487, ChEBI:CHEBI:77826; EC=1.14.11.24;
CC Evidence={ECO:0000269|PubMed:11346963};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12201;
CC Evidence={ECO:0000269|PubMed:11346963};
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 -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000250|UniProtKB:Q5W726};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: Up-regulated by iron deficiency and down-regulated by iron.
CC Not induced by anaerobic conditions. {ECO:0000269|PubMed:11117263,
CC ECO:0000269|PubMed:11346963, ECO:0000269|PubMed:8019781,
CC ECO:0000269|PubMed:9489019}.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB024058; BAA75493.1; -; mRNA.
DR EMBL; AB024007; BAB07798.1; -; Genomic_DNA.
DR EMBL; D37796; BAA07042.1; -; Genomic_DNA.
DR PIR; T05743; T05743.
DR PIR; T05903; T05903.
DR AlphaFoldDB; Q40062; -.
DR SMR; Q40062; -.
DR EnsemblPlants; HORVU.MOREX.r2.4HG0341060.1; HORVU.MOREX.r2.4HG0341060.1; HORVU.MOREX.r2.4HG0341060.
DR Gramene; HORVU.MOREX.r2.4HG0341060.1; HORVU.MOREX.r2.4HG0341060.1; HORVU.MOREX.r2.4HG0341060.
DR KEGG; ag:BAA75493; -.
DR BioCyc; MetaCyc:MON-13953; -.
DR BRENDA; 1.14.11.24; 2687.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0033760; F:2'-deoxymugineic-acid 2'-dioxygenase activity; IDA:UniProtKB.
DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0010041; P:response to iron(III) ion; IDA: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 Cytoplasm; Dioxygenase; Direct protein sequencing; Iron; Metal-binding;
KW Oxidoreductase; Vitamin C.
FT CHAIN 1..339
FT /note="2'-deoxymugineic-acid 2'-dioxygenase"
FT /id="PRO_0000389553"
FT DOMAIN 184..284
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 209
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 211
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 265
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 275
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT VARIANT 11
FT /note="H -> P (in strain: cv. Ehimehadaka No.1)"
FT VARIANT 117
FT /note="K -> R (in strain: cv. Igri)"
FT VARIANT 174
FT /note="Q -> R (in strain: cv. Ehimehadaka No.1 and cv.
FT Igri)"
FT VARIANT 261
FT /note="K -> R (in strain: cv. Igri)"
FT VARIANT 272
FT /note="A -> V (in strain: cv. Igri)"
FT VARIANT 299
FT /note="K -> E (in strain: cv. Igri)"
FT VARIANT 308
FT /note="T -> I (in strain: cv. Igri)"
SQ SEQUENCE 339 AA; 37732 MW; C5A315F018A6A03F CRC64;
MENILHATPA HVSLPESFVF ASDKVPPATK AVVSLPIIDL SCGRDEVRRS ILEAGKELGF
FQVVNHGVSK QVMRDMEGMC EQFFHLPAAD KASLYSEERH KPNRLFSGAT YDTGGEKYWR
DCLRLACPFP VDDSINEWPD TPKGLRDVIE KFTSQTRDVG KELLRLLCEG MGIQADYFEG
DLSGGNVILN INHYPSCPNP DKALGQPPHC DRNLITLLLP GAVNGLEVSY KGDWIKVDPA
PNAFVVNFGQ QLEVVTNGLL KSIEHRAMTN SALARTSVAT FIMPTQECLI GPAKEFLSKE
NPPCYRTTMF RDFMRIYNVV KLGSSLNLTT NLKNVQKEI
