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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
 
 
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