DMS1A_WHEAT
ID DMS1A_WHEAT Reviewed; 314 AA.
AC W5DYE3; Q0PCF3;
DT 22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT 19-MAR-2014, sequence version 1.
DT 03-AUG-2022, entry version 52.
DE RecName: Full=Deoxymugineic acid synthase 1-A {ECO:0000303|PubMed:16926158, ECO:0000303|PubMed:28475636};
DE Short=TaDMAS1 {ECO:0000303|PubMed:16926158};
DE EC=1.1.1.285 {ECO:0000269|PubMed:16926158};
GN Name=DMAS1-A {ECO:0000303|PubMed:28475636};
GN Synonyms=DMAS1 {ECO:0000303|PubMed:16926158};
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 [MRNA], FUNCTION, PATHWAY, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND INDUCTION BY IRON-DEFICIENCY.
RC STRAIN=cv. Chinese Spring;
RX PubMed=16926158; DOI=10.1074/jbc.m604133200;
RA Bashir K., Inoue H., Nagasaka S., Takahashi M., Nakanishi H., Mori S.,
RA Nishizawa N.K.;
RT "Cloning and characterization of deoxymugineic acid synthase genes from
RT graminaceous plants.";
RL J. Biol. Chem. 281:32395-32402(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, AND INDUCTION BY
RP IRON-DEFICIENCY.
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chinese Spring;
RX PubMed=23192148; DOI=10.1038/nature11650;
RA Brenchley R., Spannagl M., Pfeifer M., Barker G.L., D'Amore R., Allen A.M.,
RA McKenzie N., Kramer M., Kerhornou A., Bolser D., Kay S., Waite D.,
RA Trick M., Bancroft I., Gu Y., Huo N., Luo M.C., Sehgal S., Gill B.,
RA Kianian S., Anderson O., Kersey P., Dvorak J., McCombie W.R., Hall A.,
RA Mayer K.F., Edwards K.J., Bevan M.W., Hall N.;
RT "Analysis of the bread wheat genome using whole-genome shotgun
RT sequencing.";
RL Nature 491:705-710(2012).
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:0000269|PubMed:16926158}.
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:0000269|PubMed:16926158};
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:0000269|PubMed:16926158};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8-9. {ECO:0000269|PubMed:16926158};
CC -!- PATHWAY: Siderophore biosynthesis. {ECO:0000269|PubMed:16926158}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in root tissues, observed in
CC mesocotyl and embryonic roots, seedling roots, crown and seedling
CC leafes, mature bracts, anthers, pistil, caryopsis and embryos.
CC {ECO:0000269|PubMed:28475636}.
CC -!- INDUCTION: Up-regulated under iron-deficient conditions in root and
CC shoot tissues. {ECO:0000269|PubMed:16926158,
CC ECO:0000269|PubMed:28475636}.
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
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DR EMBL; AB269908; BAF03163.1; -; mRNA.
DR EMBL; KX348551; ARQ30105.1; -; Genomic_DNA.
DR AlphaFoldDB; W5DYE3; -.
DR SMR; W5DYE3; -.
DR STRING; 4565.Traes_4AS_887399584.1; -.
DR PRIDE; W5DYE3; -.
DR EnsemblPlants; TraesCAD_scaffold_127405_01G000200.1; TraesCAD_scaffold_127405_01G000200.1; TraesCAD_scaffold_127405_01G000200.
DR EnsemblPlants; TraesCLE_scaffold_069270_01G000100.1; TraesCLE_scaffold_069270_01G000100.1; TraesCLE_scaffold_069270_01G000100.
DR EnsemblPlants; TraesCS4A02G074800.1; TraesCS4A02G074800.1; TraesCS4A02G074800.
DR EnsemblPlants; TraesPAR_scaffold_077182_01G000100.1; TraesPAR_scaffold_077182_01G000100.1; TraesPAR_scaffold_077182_01G000100.
DR EnsemblPlants; TraesROB_scaffold_084192_01G000100.1; TraesROB_scaffold_084192_01G000100.1; TraesROB_scaffold_084192_01G000100.
DR EnsemblPlants; TraesWEE_scaffold_081049_01G000100.1; TraesWEE_scaffold_081049_01G000100.1; TraesWEE_scaffold_081049_01G000100.
DR Gramene; TraesCAD_scaffold_127405_01G000200.1; TraesCAD_scaffold_127405_01G000200.1; TraesCAD_scaffold_127405_01G000200.
DR Gramene; TraesCLE_scaffold_069270_01G000100.1; TraesCLE_scaffold_069270_01G000100.1; TraesCLE_scaffold_069270_01G000100.
DR Gramene; TraesCS4A02G074800.1; TraesCS4A02G074800.1; TraesCS4A02G074800.
DR Gramene; TraesPAR_scaffold_077182_01G000100.1; TraesPAR_scaffold_077182_01G000100.1; TraesPAR_scaffold_077182_01G000100.
DR Gramene; TraesROB_scaffold_084192_01G000100.1; TraesROB_scaffold_084192_01G000100.1; TraesROB_scaffold_084192_01G000100.
DR Gramene; TraesWEE_scaffold_081049_01G000100.1; TraesWEE_scaffold_081049_01G000100.1; TraesWEE_scaffold_081049_01G000100.
DR eggNOG; KOG1577; Eukaryota.
DR HOGENOM; CLU_023205_0_0_1; -.
DR OMA; CAHFYQN; -.
DR Proteomes; UP000019116; Unplaced.
DR ExpressionAtlas; W5DYE3; baseline and differential.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0033707; F:3''-deamino-3''-oxonicotianamine reductase activity; IDA:UniProtKB.
DR GO; GO:0004032; F:alditol:NADP+ 1-oxidoreductase activity; IBA:GO_Central.
DR GO; GO:1990641; P:response to iron ion starvation; IEP:UniProtKB.
DR GO; GO:0019290; P:siderophore biosynthetic process; IDA: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 1: Evidence at protein level;
KW Iron; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..314
FT /note="Deoxymugineic acid synthase 1-A"
FT /id="PRO_0000442302"
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"
FT CONFLICT 6
FT /note="K -> R (in Ref. 1; BAF03163)"
FT /evidence="ECO:0000305"
FT CONFLICT 129
FT /note="E -> D (in Ref. 1; BAF03163)"
FT /evidence="ECO:0000305"
FT CONFLICT 166
FT /note="E -> D (in Ref. 1; BAF03163)"
FT /evidence="ECO:0000305"
FT CONFLICT 216
FT /note="W -> R (in Ref. 1; BAF03163)"
FT /evidence="ECO:0000305"
FT CONFLICT 279
FT /note="H -> R (in Ref. 1; BAF03163)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 314 AA; 35198 MW; 5AE7AA7B5D7FCFBD CRC64;
MGAGDKTAAG MPRIGMGTAV QGPKPDPIRR AVLRAIEVGY RHFDTAAHYE TEAPIGEAAA
EAVRSGAVAS RDDLFITSKL WCSDAHRDRV VPALRQTLRN LQMEYVDLYL VHWPVSMKPG
RFKAPFTAED FVPFDMRAVW EAMEECHRLG LAKAIGVANF SCKKLETLLS FATIPPTVNQ
VEVNPVWQQR KLREFCRGKG IQLCAYSPLG AKGTHWGSDA VMDAGVLQEI AASRGKSVAQ
VCLRWVYEQG DCLIVKSFDE ARMRENLDVD GWELTEEEHR RIAEIPQRKI NLGKRYVSEH
GPYKSLEELW DGEI
