DMAS1_MAIZE
ID DMAS1_MAIZE Reviewed; 314 AA.
AC B4F9A4; Q0PCF2;
DT 22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Deoxymugineic acid synthase 1 {ECO:0000303|PubMed:16926158};
DE Short=ZmDMAS1 {ECO:0000303|PubMed:16926158};
DE EC=1.1.1.285 {ECO:0000269|PubMed:16926158};
GN Name=DMAS1 {ECO:0000303|PubMed:16926158};
GN ORFNames=ZEAMMB73_Zm00001d028360 {ECO:0000312|EMBL:ONL95785.1};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, PATHWAY, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND INDUCTION BY IRON-DEFICIENCY.
RC STRAIN=cv. Alice;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. B73; TISSUE=Seedling;
RX PubMed=19965430; DOI=10.1126/science.1178534;
RA Schnable P.S., Ware D., Fulton R.S., Stein J.C., Wei F., Pasternak S.,
RA Liang C., Zhang J., Fulton L., Graves T.A., Minx P., Reily A.D.,
RA Courtney L., Kruchowski S.S., Tomlinson C., Strong C., Delehaunty K.,
RA Fronick C., Courtney B., Rock S.M., Belter E., Du F., Kim K., Abbott R.M.,
RA Cotton M., Levy A., Marchetto P., Ochoa K., Jackson S.M., Gillam B.,
RA Chen W., Yan L., Higginbotham J., Cardenas M., Waligorski J., Applebaum E.,
RA Phelps L., Falcone J., Kanchi K., Thane T., Scimone A., Thane N., Henke J.,
RA Wang T., Ruppert J., Shah N., Rotter K., Hodges J., Ingenthron E.,
RA Cordes M., Kohlberg S., Sgro J., Delgado B., Mead K., Chinwalla A.,
RA Leonard S., Crouse K., Collura K., Kudrna D., Currie J., He R.,
RA Angelova A., Rajasekar S., Mueller T., Lomeli R., Scara G., Ko A.,
RA Delaney K., Wissotski M., Lopez G., Campos D., Braidotti M., Ashley E.,
RA Golser W., Kim H., Lee S., Lin J., Dujmic Z., Kim W., Talag J., Zuccolo A.,
RA Fan C., Sebastian A., Kramer M., Spiegel L., Nascimento L., Zutavern T.,
RA Miller B., Ambroise C., Muller S., Spooner W., Narechania A., Ren L.,
RA Wei S., Kumari S., Faga B., Levy M.J., McMahan L., Van Buren P.,
RA Vaughn M.W., Ying K., Yeh C.-T., Emrich S.J., Jia Y., Kalyanaraman A.,
RA Hsia A.-P., Barbazuk W.B., Baucom R.S., Brutnell T.P., Carpita N.C.,
RA Chaparro C., Chia J.-M., Deragon J.-M., Estill J.C., Fu Y., Jeddeloh J.A.,
RA Han Y., Lee H., Li P., Lisch D.R., Liu S., Liu Z., Nagel D.H., McCann M.C.,
RA SanMiguel P., Myers A.M., Nettleton D., Nguyen J., Penning B.W.,
RA Ponnala L., Schneider K.L., Schwartz D.C., Sharma A., Soderlund C.,
RA Springer N.M., Sun Q., Wang H., Waterman M., Westerman R., Wolfgruber T.K.,
RA Yang L., Yu Y., Zhang L., Zhou S., Zhu Q., Bennetzen J.L., Dawe R.K.,
RA Jiang J., Jiang N., Presting G.G., Wessler S.R., Aluru S.,
RA Martienssen R.A., Clifton S.W., McCombie W.R., Wing R.A., Wilson R.K.;
RT "The B73 maize genome: complexity, diversity, and dynamics.";
RL Science 326:1112-1115(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. B73;
RX PubMed=19936069; DOI=10.1371/journal.pgen.1000740;
RA Soderlund C., Descour A., Kudrna D., Bomhoff M., Boyd L., Currie J.,
RA Angelova A., Collura K., Wissotski M., Ashley E., Morrow D., Fernandes J.,
RA Walbot V., Yu Y.;
RT "Sequencing, mapping, and analysis of 27,455 maize full-length cDNAs.";
RL PLoS Genet. 5:E1000740-E1000740(2009).
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 -!- 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; AB269909; BAF03164.1; -; mRNA.
DR EMBL; CM007647; ONL95785.1; -; Genomic_DNA.
DR EMBL; BT033692; ACF78697.1; -; mRNA.
DR RefSeq; NP_001105931.1; NM_001112461.1.
DR AlphaFoldDB; B4F9A4; -.
DR SMR; B4F9A4; -.
DR STRING; 4577.GRMZM2G060952_P01; -.
DR PaxDb; B4F9A4; -.
DR EnsemblPlants; Zm00001eb010040_T003; Zm00001eb010040_P003; Zm00001eb010040.
DR GeneID; 778439; -.
DR Gramene; Zm00001eb010040_T003; Zm00001eb010040_P003; Zm00001eb010040.
DR KEGG; zma:778439; -.
DR eggNOG; KOG1577; Eukaryota.
DR OMA; TYNTGER; -.
DR OrthoDB; 1016440at2759; -.
DR Proteomes; UP000007305; Chromosome 1.
DR ExpressionAtlas; B4F9A4; 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: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; 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..314
FT /note="Deoxymugineic acid synthase 1"
FT /id="PRO_0000442300"
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 14
FT /note="I -> V (in Ref. 1; BAF03164)"
FT /evidence="ECO:0000305"
FT CONFLICT 311
FT /note="D -> A (in Ref. 1; BAF03164)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 314 AA; 35378 MW; 14A3565818B357ED CRC64;
MSATGRAPCG LPRIGLGTAV QGPRPDPVRA AVLRAIQLGY RHFDTAAHYA TEAPIGEAAA
EAVRTGLVAS REDLFVTSKV WCADAHRDRV LPALRRTLSN LQMEYVDLYM VHWPVTMKAG
RFTAPFTPED FEPFDMRAVW EAMEECHRLG LAKAIGVCNF SCKKLETLLS FATIPPVVNQ
VEINPVWQQR KLREFCRAKG IQLCAYSPLG AKGTHWGSDS VMDSGVLHEI AKSKGKTVAQ
VCLRWVYEQG DCLIVKSFDE GRMKENLDIV DWELSEEERQ RISKIPQRKI NQGRRYVSEH
GPYKSFEELW DGEI
