IDS2_HORVU
ID IDS2_HORVU Reviewed; 338 AA.
AC Q40061;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Mugineic-acid 3-dioxygenase;
DE EC=1.14.11.25;
DE AltName: Full=Protein iron deficiency-specific 2;
GN Name=IDS2;
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 [GENOMIC DNA], TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=cv. NK 1558;
RX PubMed=8061321; DOI=10.1007/bf00029608;
RA Okumura N., Nishizawa N., Umehara Y., Ohata T., Nakanishi H., Yamaguchi T.,
RA Chino M., Mori S.;
RT "A dioxygenase gene (Ids2) expressed under iron deficiency conditions in
RT the roots of Hordeum vulgare.";
RL Plant Mol. Biol. 25:705-719(1994).
RN [2]
RP FUNCTION.
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 TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=17467282; DOI=10.1016/j.plaphy.2007.03.007;
RA Kobayashi T., Yoshihara T., Itai R.N., Nakanishi H., Takahashi M., Mori S.,
RA Nishizawa N.K.;
RT "Promoter analysis of iron-deficiency-inducible barley IDS3 gene in
RT Arabidopsis and tobacco plants.";
RL Plant Physiol. Biochem. 45:262-269(2007).
RN [4]
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-3 positions of mugineic acid (MA)
CC and 2'-deoxymugineic acid (DMA). May be involved in boron tolerance.
CC {ECO:0000269|PubMed:11117263, ECO:0000269|PubMed:17478636}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + mugineate + O2 = 3-epihydroxymugineate + CO2
CC + H(+) + succinate; Xref=Rhea:RHEA:14509, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:58488, ChEBI:CHEBI:77826;
CC EC=1.14.11.25;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2'-deoxymugineate + 2-oxoglutarate + O2 = 3-epihydroxy-2'-
CC deoxymugineate + CO2 + H(+) + succinate; Xref=Rhea:RHEA:20065,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:58487,
CC ChEBI:CHEBI:58684; EC=1.14.11.25;
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; Evidence={ECO:0000250};
CC -!- TISSUE SPECIFICITY: Expressed in roots, but not in leaves.
CC {ECO:0000269|PubMed:17467282, ECO:0000269|PubMed:8061321}.
CC -!- INDUCTION: Up-regulated by manganese and zinc deficiency or by excess
CC NaCl. Down-regulated by iron. {ECO:0000269|PubMed:17467282,
CC ECO:0000269|PubMed:8061321}.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; D15051; BAA03647.1; -; Genomic_DNA.
DR PIR; S47972; S47972.
DR AlphaFoldDB; Q40061; -.
DR SMR; Q40061; -.
DR EnsemblPlants; HORVU.MOREX.r2.7HG0623950.1; HORVU.MOREX.r2.7HG0623950.1; HORVU.MOREX.r2.7HG0623950.
DR Gramene; HORVU.MOREX.r2.7HG0623950.1; HORVU.MOREX.r2.7HG0623950.1; HORVU.MOREX.r2.7HG0623950.
DR KEGG; ag:BAA03647; -.
DR OMA; CHPLEQW; -.
DR BioCyc; MetaCyc:MON-13971; -.
DR GO; GO:0052860; F:2'-deoxymugineic-acid 3-dioxygenase activity; IEA:UniProtKB-EC.
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:0033761; F:mugineic-acid 3-dioxygenase activity; IEA:UniProtKB-EC.
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 2: Evidence at transcript level;
KW Dioxygenase; Iron; Metal-binding; Oxidoreductase; Vitamin C.
FT CHAIN 1..338
FT /note="Mugineic-acid 3-dioxygenase"
FT /id="PRO_0000389552"
FT DOMAIN 180..283
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 208
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 210
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 264
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 274
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ SEQUENCE 338 AA; 37574 MW; 1AB93EB5B757A919 CRC64;
MAKVMNLTPV HASSIPDSFL LPADRLHPAT TDVSLPIIDM SRGRDEVRQA ILDSGKEYGF
IQVVNHGISE PMLHEMYAVC HEFFDMPAED KAEFFSEDRS ERNKLFCGSA FETLGEKYWI
DVLELLYPLP SGDTKDWPHK PQMLREVVGN YTSLARGVAM EILRLLCEGL GLRPDFFVGD
ISGGRVVVDI NYYPPSPNPS RTLGLPPHCD RDLMTVLLPG AVPGLEIAYK GGWIKVQPVP
NSLVINFGLQ LEVVTNGYLK AVEHRAATNF AEPRLSVASF IVPADDCVVG PAEEFVSEDN
PPRYRTLTVG EFKRKHNVVN LDSSINQIIN INNNQKGI
