DMAS1_HORVU
ID DMAS1_HORVU Reviewed; 314 AA.
AC Q0PCF4;
DT 22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Deoxymugineic acid synthase 1 {ECO:0000303|PubMed:16926158};
DE Short=HvDMAS1 {ECO:0000303|PubMed:16926158};
DE EC=1.1.1.285 {ECO:0000269|PubMed:16667646, ECO:0000269|PubMed:16926158};
GN Name=DMAS1 {ECO:0000303|PubMed:16926158};
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], FUNCTION, PATHWAY, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND INDUCTION BY IRON-DEFICIENCY.
RC STRAIN=cv. Ehimehadaka No.1;
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 FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND CATALYTIC ACTIVITY.
RC STRAIN=cv. Ehimehadakamugi No. 1;
RX PubMed=16667646; DOI=10.1104/pp.93.4.1497;
RA Shojima S., Nishizawa N.-K., Fushiya S., Nozoe S., Irifune T., Mori S.;
RT "Biosynthesis of phytosiderophores: in vitro biosynthesis of 2'-
RT deoxymugineic acid from l-methionine and nicotianamine.";
RL Plant Physiol. 93:1497-1503(1990).
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:16667646,
CC 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:16667646, 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:16667646, ECO:0000269|PubMed:16926158};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8-9. {ECO:0000269|PubMed:16667646,
CC ECO:0000269|PubMed:16926158};
CC -!- PATHWAY: Siderophore biosynthesis. {ECO:0000269|PubMed:16926158}.
CC -!- INDUCTION: Up-regulated under iron-deficient conditions in root
CC tissues. {ECO:0000269|PubMed:16926158}.
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
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DR EMBL; AB269907; BAF03162.1; -; mRNA.
DR AlphaFoldDB; Q0PCF4; -.
DR SMR; Q0PCF4; -.
DR PRIDE; Q0PCF4; -.
DR BioCyc; MetaCyc:MON-13968; -.
DR ExpressionAtlas; Q0PCF4; baseline and differential.
DR GO; GO:0033707; F:3''-deamino-3''-oxonicotianamine reductase activity; IDA:UniProtKB.
DR GO; GO:0034224; P:cellular response to zinc ion starvation; IEA:EnsemblPlants.
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.
FT CHAIN 1..314
FT /note="Deoxymugineic acid synthase 1"
FT /id="PRO_0000442301"
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 SITE 79
FT /note="Lowers pKa of active site Tyr"
FT /evidence="ECO:0000255|PIRSR:PIRSR000097-3"
SQ SEQUENCE 314 AA; 35155 MW; B5C186D083711581 CRC64;
MGAGDRTVAG MPRIGMGTAV QGPKPDPIRR AVLRAIEIGY RHFDTAAHYE TEAPIGEAAA
EAVRSGAVAS RDDLFITSKL WCSDAHGDRV VPALRHTLRN LQMEYVDLYL VHWPVSMKPG
RFKAPFTAED FVPFDMRAVW EAMEECHRLG LAKAIGVANF SCKKLDTLLS FATIPPTVNQ
VEVNPVWQQR KLREFCRGKG IQLCAYSPLG AKGTHWGSDA VMDAGVLQDI AASRGKSVAQ
VCLRWVYEQG DCLIVKSFDE ARMRENLDVD GWELTEEERR RIAEIPQRKI NLGKRYVSDH
GPYKSLEELW DGEI
