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Information on EC 2.6.1.80 - nicotianamine aminotransferase
for references in articles please use BRENDA:EC2.6.1.80
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EC Tree 2 Transferases
2.6 Transferring nitrogenous groups
2.6.1 Transaminases
2.6.1.80 nicotianamine aminotransferase
IUBMB Comments
A pyridoxal-phosphate protein. This enzyme is produced by grasses. They secrete both the nicotianamine and the transaminated product into the soil around them. Both compounds chelate iron(II) and iron(III); these chelators, called mugineic acid family phytosiderophores, are taken up by the grass, which is thereby supplied with iron.
The enzyme appears in viruses and cellular organisms
- 2.6.1.80
-
phytosiderophores
- barley
- shoot
-
graminaceous
- osnas1
- agriculture
-
osirt1
-
fe-deficient
-
mugineic
-
fe-sufficient
-
deoxymugineic
-
deficiency-induced
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rhizosphere
-
osysl15
-
feiii
-
osnramp1
-
calcareous
-
atfro2
-
iron-deficient
-
pericycle
-
petis
Reaction Schemes
showSynonyms
osnaat1, nicotianamine aminotransferase, naat-b, tanaat, naat-a, naat1, naat2-d, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
naat-B
nicotianamine aminotransferase 1
-
nicotianamine transaminase
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
nicotianamine + 2-oxoglutarate = 3''-deamino-3''-oxonicotianamine + L-glutamate
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
2'-deoxymugineic acid phytosiderophore biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
nicotianamine:2-oxoglutarate aminotransferase
A pyridoxal-phosphate protein. This enzyme is produced by grasses. They secrete both the nicotianamine and the transaminated product into the soil around them. Both compounds chelate iron(II) and iron(III); these chelators, called mugineic acid family phytosiderophores, are taken up by the grass, which is thereby supplied with iron.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
Substrates: a point mutation in a gene encoding nicotianamine aminotransferase (NAAT1) stimulates the Fe(II) acquisition system and leads to iron accumulation in rice
Products: -
Products: -
?
nicotianamine + 2-oxoglutarate
3''-deamino-3''-oxonicotianamine + L-glutamate
-
Substrates: -
Products: -
Products: -
?
nicotianamine + 2-oxoglutarate
3''-deamino-3''-oxonicotianamine + L-glutamate
Substrates: -
Products: -
Products: -
?
nicotianamine + 2-oxoglutarate
3''-deamino-3''-oxonicotianamine + L-glutamate
Substrates: -
Products: -
Products: -
?
nicotianamine + 2-oxoglutarate
3''-deamino-3''-oxonicotianamine + L-glutamate
A0A1D5SSY7, A0A1D5RWZ6, A0A1D5SWF7, A0A1D5RTF7, A0A1X9QHI5, A0A1X9QHH3
Substrates: -
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
Substrates: a point mutation in a gene encoding nicotianamine aminotransferase (NAAT1) stimulates the Fe(II) acquisition system and leads to iron accumulation in rice
Products: -
Products: -
?
nicotianamine + 2-oxoglutarate
3''-deamino-3''-oxonicotianamine + L-glutamate
-
Substrates: -
Products: -
Products: -
?
nicotianamine + 2-oxoglutarate
3''-deamino-3''-oxonicotianamine + L-glutamate
Substrates: -
Products: -
Products: -
?
nicotianamine + 2-oxoglutarate
3''-deamino-3''-oxonicotianamine + L-glutamate
Substrates: -
Products: -
Products: -
?
nicotianamine + 2-oxoglutarate
3''-deamino-3''-oxonicotianamine + L-glutamate
A0A1D5SSY7, A0A1D5RWZ6, A0A1D5SWF7, A0A1D5RTF7, A0A1X9QHI5, A0A1X9QHH3
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
A0A1D5SSY7, A0A1D5RWZ6, A0A1D5SWF7, A0A1D5RTF7, A0A1X9QHI5, A0A1X9QHH3
mature, very low expression level
brenda
OsNAAT1 is induced in all the cells of Fe-deficient leaves
brenda
A0A1D5SSY7, A0A1D5RWZ6, A0A1D5SWF7, A0A1D5RTF7, A0A1X9QHI5, A0A1X9QHH3
very low expression level
brenda
A0A1D5SSY7, A0A1D5RWZ6, A0A1D5SWF7, A0A1D5RTF7, A0A1X9QHI5, A0A1X9QHH3
very low expression level
brenda
OsNAAT1, but not OsNAAT2-6, is strongly up-regulated by Fe deficiency, both in roots and shoots. OsNAAT1 is expressed in companion and pericycle cells adjacent to the protoxylem of Fe-sufficient roots
brenda
OsNAAT1, but not OsNAAT2-6, is strongly up-regulated by Fe deficiency, both in roots and shoots
brenda
A0A1D5SSY7, A0A1D5RWZ6, A0A1D5SWF7, A0A1D5RTF7, A0A1X9QHI5, A0A1X9QHH3
from seedling and embryo, high expression level
brenda
A0A1D5SSY7, A0A1D5RWZ6, A0A1D5SWF7, A0A1D5RTF7, A0A1X9QHI5, A0A1X9QHH3
from seedling and embryo
brenda
OsNAAT1, but not OsNAAT2-6, is strongly up-regulated by Fe deficiency, both in roots and shoots. OsNAAT1 expression is observed in the companion cells of Fe-sufficient shoots
brenda
OsNAAT1, but not OsNAAT2-6, is strongly up-regulated by Fe deficiency, both in roots and shoots
brenda
additional information
TaNAAT2 genes are expressed at highest levels in anther tissues whilst the TaNAAT1 genes are expressed at highest levels in root tissues of bread wheat, tissue expression profile, overview
brenda
additional information
TaNAAT2 genes are expressed at highest levels in anther tissues whilst the TaNAAT1 genes are expressed at highest levels in root tissues of bread wheat, tissue expression profile, overview
brenda
additional information
A0A1D5SWF7
TaNAAT2 genes are expressed at highest levels in anther tissues whilst the TaNAAT1 genes are expressed at highest levels in root tissues of bread wheat, tissue expression profile, overview
brenda
additional information
TaNAAT2 genes are expressed at highest levels in anther tissues whilst the TaNAAT1 genes are expressed at highest levels in root tissues of bread wheat, tissue expression profile, overview
brenda
additional information
TaNAAT2 genes are expressed at highest levels in anther tissues whilst the TaNAAT1 genes are expressed at highest levels in root tissues of bread wheat, tissue expression profile, overview
brenda
additional information
TaNAAT2 genes are expressed at highest levels in anther tissues whilst the TaNAAT1 genes are expressed at highest levels in root tissues of bread wheat, tissue expression profile, overview
brenda
additional information
-
TaNAAT2 genes are expressed at highest levels in anther tissues whilst the TaNAAT1 genes are expressed at highest levels in root tissues of bread wheat, tissue expression profile, overview
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
A0A1D5SSY7, A0A1D5RWZ6, A0A1D5SWF7, A0A1D5RTF7, A0A1X9QHI5, A0A1X9QHH3
sequence structure and length of the TaNAAT1, TaNAAT2 and TaDMAS1 genes in Triticum aestivum cv. Gladius, comparison, phylogenetic tree, overview
metabolism
A0A1D5SSY7, A0A1D5RWZ6, A0A1D5SWF7, A0A1D5RTF7, A0A1X9QHI5, A0A1X9QHH3
iron (Fe) uptake in graminaceous plant species occurs via the release and uptake of Fe-chelating compounds known as mugineic acid family phytosiderophores (MAs). In the MAs biosynthetic pathway, nicotianamine aminotransferase (NAAT) and deoxymugineic acid synthase (DMAS, EC 1.1.1.285) enzymes catalyse the formation of 2'-deoxymugineic acid (DMA) from nicotianamine (NA). The TaNAAT1, TaNAAT2 and TaDMAS1 genes are differentially regulated by plant Fe status and their expression is significantly upregulated in root tissues from day five onwards during a seven-day Fe deficiency treatment. Expression levels of the TaNAAT1, TaNAAT2, and TaDMAS1 genes are temporally regulated in wheat roots to enable rapid DMA biosynthesis in response to Fe deficiency and avoid NA depletion
physiological function
A0A1D5SSY7, A0A1D5RWZ6, A0A1D5SWF7, A0A1D5RTF7, A0A1X9QHI5, A0A1X9QHH3
the nicotianamine aminotransferase and deoxymugineic acid synthase genes are essential to iron uptake in Triticum aestivum
Show AA Sequence and Transmembrane Helices (321 entries)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene NAAT1-A, genetic organization, sequence comparisons, phylogenetic tree, the three TaNAAT1 genes are located on chromosomal group 1, quantitative reverse transcription-PCR enzyme expression analysis
A0A1D5SSY7, A0A1D5RWZ6, A0A1D5SWF7, A0A1D5RTF7, A0A1X9QHI5, A0A1X9QHH3
gene NAAT1-B, genetic organization, sequence comparisons, phylogenetic tree, the three TaNAAT1 genes are located on chromosomal group 1, quantitative reverse transcription-PCR enzyme expression analysis
A0A1D5SSY7, A0A1D5RWZ6, A0A1D5SWF7, A0A1D5RTF7, A0A1X9QHI5, A0A1X9QHH3
gene NAAT1-D, genetic organization, sequence comparisons, phylogenetic tree, the three TaNAAT1 genes are located on chromosomal group 1, quantitative reverse transcription-PCR enzyme expression analysis
A0A1D5SSY7, A0A1D5RWZ6, A0A1D5SWF7, A0A1D5RTF7, A0A1X9QHI5, A0A1X9QHH3
gene NAAT2-A, genetic organization, sequence comparisons, phylogenetic tree, the three TaNAAT2 genes are located on chromosomal group 1, quantitative reverse transcription-PCR enzyme expression analysis
A0A1D5SSY7, A0A1D5RWZ6, A0A1D5SWF7, A0A1D5RTF7, A0A1X9QHI5, A0A1X9QHH3
gene NAAT2-B, genetic organization, sequence comparisons, phylogenetic tree, the three TaNAAT2 genes are located on chromosomal group 1, quantitative reverse transcription-PCR enzyme expression analysis
A0A1D5SSY7, A0A1D5RWZ6, A0A1D5SWF7, A0A1D5RTF7, A0A1X9QHI5, A0A1X9QHH3
gene NAAT2-D, genetic organization, sequence comparisons, phylogenetic tree, the three TaNAAT2 genes are located on chromosomal group 1, quantitative reverse transcription-PCR enzyme expression analysis
A0A1D5SSY7, A0A1D5RWZ6, A0A1D5SWF7, A0A1D5RTF7, A0A1X9QHI5, A0A1X9QHH3
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
TaNAAT1 and TaNAAT2 genes are differentially regulated by plant Fe status and their expression is significantly upregulated in root tissues from day five onwards during a seven-day Fe deficiency treatment
A0A1D5SSY7, A0A1D5RWZ6, A0A1D5SWF7, A0A1D5RTF7, A0A1X9QHI5, A0A1X9QHH3
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
agriculture
production of biofortified rice via introduction of the soybean ferritin gene (Soyfer H2) driven by two endosperm-specific promoters, along with the barley nicotianamine synthase gene NAS1, two nicotianamine aminotransferase genes Naat-A and Naat-B, and a mugineic acid synthase gene IDS3 to enhance mugineic acid production in rice plants. Lines expressing both ferritin and mugineic acid biosynthetic genes show signs of iron-deficiency tolerance in calcareous soil. The iron concentration in polished T3 seeds is increased by 4- and 2.5times, respectively
agriculture
A0A1D5SSY7, A0A1D5RWZ6, A0A1D5SWF7, A0A1D5RTF7, A0A1X9QHI5, A0A1X9QHH3
the TaNAAT1, TaNAAT2 and TaDMAS1 genes provides a valuable genetic resource for improving bread wheat growth on Fe deficient soils and enhancing grain Fe nutrition
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kanazawa, K.; Higuchi, K.; Nishizawa, N.K.; Fushiya, S.; Mori, S.
Detection of two distinct isoenzymes of nicotianamine aminotransferase in Fe-deficient barley roots
J. Exp. Bot.
46
1241-1244
1995
Hordeum vulgare
-
brenda
Takahashi, M.; Nakanishi, H.; Kawasaki, S.; Nishizawa, N.K.; Mori, S.
Enhanced tolerance of rice to low iron availability in alkaline soils using barley nicotianamine aminotransferase genes
Nat. Biotechnol.
19
466-469
2001
Hordeum vulgare, Hordeum vulgare (Q9ST02)
brenda
Takahashi, M.; Yamaguchi, H.; Nakanishi, H.; Shioiri, T.; Nishizawa, N.K.; Mori, S.
Cloning two genes for nicotianamine aminotransferase, a critical enzyme in iron acquisition (Strategy II) in graminaceous plants
Plant Physiol.
121
947-956
1999
Hordeum vulgare, Hordeum vulgare (Q9ST02), Hordeum vulgare (Q9ST03)
brenda
Inoue, H.; Takahashi, M.; Kobayashi, T.; Suzuki, M.; Nakanishi, H.; Mori, S.; Nishizawa, N.K.
Identification and localisation of the rice nicotianamine aminotransferase gene OsNAAT1 expression suggests the site of phytosiderophore synthesis in rice
Plant Mol. Biol.
66
193-203
2008
Oryza sativa, Oryza sativa (Q6K2Y8), Oryza sativa (Q6K4T7), Oryza sativa (Q0IS70)
brenda
Cheng, L.; Wang, F.; Shou, H.; Huang, F.; Zheng, L.; He, F.; Li, J.; Zhao, F.J.; Ueno, D.; Ma, J.F.; Wu, P.
Mutation in nicotianamine aminotransferase stimulated the Fe(II) acquisition system and led to iron accumulation in rice
Plant Physiol.
145
1647-1657
2007
Oryza sativa
brenda
Masuda, H.; Kobayashi, T.; Ishimaru, Y.; Takahashi, M.; Aung, M.S.; Nakanishi, H.; Mori, S.; Nishizawa, N.K.
Iron-biofortification in rice by the introduction of three barley genes participated in mugineic acid biosynthesis with soybean ferritin gene
Front. Plant Sci.
4
132
2013
Hordeum vulgare (Q9ST02), Hordeum vulgare (Q9ST03), Hordeum vulgare
brenda
Beasley, J.T.; Bonneau, J.P.; Johnson, A.A.T.
Characterisation of the nicotianamine aminotransferase and deoxymugineic acid synthase genes essential to Strategy II iron uptake in bread wheat (Triticum aestivum L.)
PLoS ONE
12
e0177061
2017
Triticum aestivum (A0A1D5SSY7), Triticum aestivum (A0A1D5RWZ6), Triticum aestivum (A0A1D5SWF7), Triticum aestivum (A0A1D5RTF7), Triticum aestivum (A0A1X9QHI5), Triticum aestivum (A0A1X9QHH3), Triticum aestivum
brenda
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