DMS1D_WHEAT
ID DMS1D_WHEAT Reviewed; 314 AA.
AC A0A1X9QHJ0;
DT 22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2017, sequence version 1.
DT 03-AUG-2022, entry version 20.
DE RecName: Full=Deoxymugineic acid synthase 1-D {ECO:0000303|PubMed:28475636};
DE EC=1.1.1.285 {ECO:0000250|UniProtKB:W5DYE3};
GN Name=DMAS1-D {ECO:0000303|PubMed:28475636};
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Gladius;
RX PubMed=28475636; DOI=10.1371/journal.pone.0177061;
RA Beasley J.T., Bonneau J.P., Johnson A.A.T.;
RT "Characterisation of the nicotianamine aminotransferase and deoxymugineic
RT acid synthase genes essential to Strategy II iron uptake in bread wheat
RT (Triticum aestivum L.).";
RL PLoS ONE 12:E0177061-E0177061(2017).
CC -!- FUNCTION: Catalyzes the reduction of a 3''-keto intermediate during the
CC biosynthesis of 2'-deoxymugineic acid (DMA) from L-Met. Involved in the
CC formation of phytosiderophores (MAs) belonging to the mugineic acid
CC family and required to acquire iron. {ECO:0000250|UniProtKB:W5DYE3}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2'-deoxymugineate + NAD(+) = 3''-deamino-3''-oxonicotianamine
CC + H(+) + NADH; Xref=Rhea:RHEA:16141, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58487,
CC ChEBI:CHEBI:58685; EC=1.1.1.285;
CC Evidence={ECO:0000250|UniProtKB:W5DYE3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2'-deoxymugineate + NADP(+) = 3''-deamino-3''-oxonicotianamine
CC + H(+) + NADPH; Xref=Rhea:RHEA:16137, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:58487,
CC ChEBI:CHEBI:58685; EC=1.1.1.285;
CC Evidence={ECO:0000250|UniProtKB:W5DYE3};
CC -!- PATHWAY: Siderophore biosynthesis. {ECO:0000250|UniProtKB:W5DYE3}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in root tissues, observed, at low
CC levels, in mesocotyl and embryonic roots, seedling roots, crown and
CC seedling leafes, mature bracts, anthers, pistil, caryopsis and embryos.
CC {ECO:0000269|PubMed:28475636}.
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
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DR EMBL; KX348553; ARQ30107.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X9QHJ0; -.
DR SMR; A0A1X9QHJ0; -.
DR STRING; 4565.Traes_4DL_01BE8F7DE.2; -.
DR eggNOG; KOG1277; Eukaryota.
DR eggNOG; KOG1577; Eukaryota.
DR Proteomes; UP000019116; Unplaced.
DR ExpressionAtlas; A0A1X9QHJ0; baseline and differential.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0033707; F:3''-deamino-3''-oxonicotianamine reductase activity; ISS:UniProtKB.
DR GO; GO:0004032; F:alditol:NADP+ 1-oxidoreductase activity; IBA:GO_Central.
DR GO; GO:1990641; P:response to iron ion starvation; ISS:UniProtKB.
DR GO; GO:0019290; P:siderophore biosynthetic process; ISS:UniProtKB.
DR CDD; cd19124; AKR_AKR4A_4B; 1.
DR Gene3D; 3.20.20.100; -; 1.
DR InterPro; IPR020471; AKR.
DR InterPro; IPR044497; AKR4A/B.
DR InterPro; IPR018170; Aldo/ket_reductase_CS.
DR InterPro; IPR023210; NADP_OxRdtase_dom.
DR InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR Pfam; PF00248; Aldo_ket_red; 1.
DR PIRSF; PIRSF000097; AKR; 1.
DR PRINTS; PR00069; ALDKETRDTASE.
DR SUPFAM; SSF51430; SSF51430; 1.
DR PROSITE; PS00798; ALDOKETO_REDUCTASE_1; 1.
DR PROSITE; PS00063; ALDOKETO_REDUCTASE_3; 1.
PE 2: Evidence at transcript level;
KW Iron; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..314
FT /note="Deoxymugineic acid synthase 1-D"
FT /id="PRO_0000442304"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 49
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q8CG76"
FT BINDING 44
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O43488"
FT BINDING 112
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8CG76"
FT BINDING 158..159
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O43488"
FT BINDING 180
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O43488"
FT BINDING 258..266
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O43488"
FT BINDING 273..281
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q8CG76"
SQ SEQUENCE 314 AA; 35216 MW; C6C5FD11F5D7AA28 CRC64;
MGAGEKTAAG MPRIGMGTAV QGPKPDPIRR AVLRAIEIGY RHFDTAAHYE TEAPIGEAAA
EAVRSGAVAS RDELFITSKL WCSDAHRDRV VPALRQSLRN LQMEYVDLYL VHWPVSMKPG
RFKAPFTAED FVPFDMRAVW EAMEECHRLG LAKAIGVANF SCKKLETLLS FATIPPTVNQ
VEVNPVWQQR KLREFCRGKG IQLCAYSPLG AKGTHWGSDA VMDAGVLQEI AASRGKSVAQ
VCLRWVYEQG DCLIVKSFDE ARMRENLEVD GWELTEEERL RIAEIPQRKI NLGKRYVSEH
GPYKSLEELW DGEI
