DMAS1_ORYSJ
ID DMAS1_ORYSJ Reviewed; 318 AA.
AC Q10PE7; Q0PCF5; Q8H011;
DT 22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Deoxymugineic acid synthase 1 {ECO:0000303|PubMed:16926158};
DE Short=OsDMAS1 {ECO:0000303|PubMed:16926158};
DE EC=1.1.1.285 {ECO:0000269|PubMed:16926158};
GN Name=DMAS1 {ECO:0000303|PubMed:16926158};
GN OrderedLocusNames=LOC_Os03g13390 {ECO:0000312|EMBL:ABF94849.1},
GN Os03g0237100 {ECO:0000312|EMBL:BAF11407.1};
GN ORFNames=OJ1081D05.5 {ECO:0000312|EMBL:AAO06971.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, PATHWAY, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION BY IRON-DEFICIENCY, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Nipponbare;
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 REVIEW.
RX PubMed=19704569; DOI=10.4161/psb.1.6.3590;
RA Bashir K., Nishizawa N.K.;
RT "Deoxymugineic Acid synthase: a gene important for fe-acquisition and
RT homeostasis.";
RL Plant Signal. Behav. 1:290-292(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16109971; DOI=10.1101/gr.3869505;
RG The rice chromosome 3 sequencing consortium;
RA Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA Jin W., Lee H.R., Jiang J., Jackson S.;
RT "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT and diverged grass species.";
RL Genome Res. 15:1284-1291(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [6]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [7]
RP DEVELOPMENTAL STAGE.
RC STRAIN=cv. Nipponbare, and cv. Tsukinohikari;
RX PubMed=17333504; DOI=10.1007/s11103-007-9132-4;
RA Nozoye T., Inoue H., Takahashi M., Ishimaru Y., Nakanishi H., Mori S.,
RA Nishizawa N.K.;
RT "The expression of iron homeostasis-related genes during rice
RT germination.";
RL Plant Mol. Biol. 64:35-47(2007).
RN [8]
RP INDUCTION BY IRON-DEFICIENCY AND ZINC-DEFICIENCY.
RX PubMed=18224446; DOI=10.1007/s11103-008-9292-x;
RA Suzuki M., Tsukamoto T., Inoue H., Watanabe S., Matsuhashi S.,
RA Takahashi M., Nakanishi H., Mori S., Nishizawa N.K.;
RT "Deoxymugineic acid increases Zn translocation in Zn-deficient rice
RT plants.";
RL Plant Mol. Biol. 66:609-617(2008).
RN [9]
RP INDUCTION BY IRON-DEFICIENCY.
RX PubMed=24887487; DOI=10.1016/j.gene.2014.05.069;
RA Agarwal S., Tripura Venkata V.G., Kotla A., Mangrauthia S.K.,
RA Neelamraju S.;
RT "Expression patterns of QTL based and other candidate genes in Madhukar x
RT Swarna RILs with contrasting levels of iron and zinc in unpolished rice
RT grains.";
RL Gene 546:430-436(2014).
RN [10]
RP REVIEW ON RESPONSES TO IRON-DEFICIENCY.
RX PubMed=26224556; DOI=10.1186/s12284-014-0027-0;
RA Kobayashi T., Nakanishi Itai R., Nishizawa N.K.;
RT "Iron deficiency responses in rice roots.";
RL Rice 7:27-27(2014).
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: Confined to cells participating in long distance
CC transport (e.g. in the parts of pericycle cells adjacent to the
CC protoxylem and metaxylem) in roots and to vascular bundles in shoots.
CC {ECO:0000269|PubMed:16926158}.
CC -!- DEVELOPMENTAL STAGE: Expressed in germinating seeds prior to protrusion
CC of the radicle, especially in the vascular bundle of the seminal root 3
CC days after sowing. {ECO:0000269|PubMed:17333504}.
CC -!- INDUCTION: Up-regulated under iron-deficient conditions in root and
CC shoot tissues (PubMed:16926158, PubMed:18224446, PubMed:24887487).
CC Slightly induced in shoots by zinc deficiency (PubMed:18224446).
CC {ECO:0000269|PubMed:16926158, ECO:0000269|PubMed:18224446,
CC ECO:0000269|PubMed:24887487}.
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO06971.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB269906; BAF03161.1; -; mRNA.
DR EMBL; AC134229; AAO06971.1; ALT_SEQ; Genomic_DNA.
DR EMBL; DP000009; ABF94849.1; -; Genomic_DNA.
DR EMBL; AP008209; BAF11407.1; -; Genomic_DNA.
DR EMBL; AP014959; BAS83157.1; -; Genomic_DNA.
DR RefSeq; XP_015630949.1; XM_015775463.1.
DR AlphaFoldDB; Q10PE7; -.
DR SMR; Q10PE7; -.
DR STRING; 4530.OS03T0237100-01; -.
DR PaxDb; Q10PE7; -.
DR PRIDE; Q10PE7; -.
DR EnsemblPlants; Os03t0237100-01; Os03t0237100-01; Os03g0237100.
DR GeneID; 4332187; -.
DR Gramene; Os03t0237100-01; Os03t0237100-01; Os03g0237100.
DR KEGG; osa:4332187; -.
DR eggNOG; KOG1577; Eukaryota.
DR HOGENOM; CLU_023205_0_0_1; -.
DR InParanoid; Q10PE7; -.
DR OMA; TYNTGER; -.
DR OrthoDB; 1016440at2759; -.
DR PlantReactome; R-OSA-9025754; Mugineic acid biosynthesis.
DR Proteomes; UP000000763; Chromosome 3.
DR Proteomes; UP000059680; Chromosome 3.
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:0034224; P:cellular response to zinc ion starvation; IEP:UniProtKB.
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; PS00062; ALDOKETO_REDUCTASE_2; 1.
DR PROSITE; PS00063; ALDOKETO_REDUCTASE_3; 1.
PE 1: Evidence at protein level;
KW Iron; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..318
FT /note="Deoxymugineic acid synthase 1"
FT /id="PRO_0000442299"
FT ACT_SITE 53
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q8CG76"
FT BINDING 48
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O43488"
FT BINDING 116
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8CG76"
FT BINDING 162..163
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O43488"
FT BINDING 184
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O43488"
FT BINDING 262..270
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O43488"
FT BINDING 277..285
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q8CG76"
FT CONFLICT 78
FT /note="L -> P (in Ref. 1; BAF03161)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 318 AA; 35422 MW; 56A77A698D609F51 CRC64;
MSDGGAGAKG AGFGMPRVGM GTAVQGPRPE PIRRAVLKAI EAGYRHFDTA AHYETEAPIG
EAAAEAVRSG AIASRADLFI TSKLWCSDAH RDRVLPALRQ TLWNLQMEYV DLYLVHWPVS
MKPGRYKAPF TADDFVPFDM RAVWEAMEEC HRLGLAKAIG VCNFSCKKLD TLLSFATIPP
AVNQVEVNPV WQQRKLRELC REKGVQICAY SPLGASGTHW GSDSVMASAV LRDIAQSKGK
TVAQVCLRWV YEQGDCLIVK SFDEARMREN LDIVGWELTE EERQRIAGIP QRKINRALRF
VSDHGPYKSL DDLWDGEI
