RecName: Full=Probable nicotianamine synthase 4; AltName: Full=S-adenosyl-L-methionine:S-adenosyl-L-methionine:S-adenosyl-methionine 3-amino-3-carboxypropyltransferase 4
Protein Classification
nicotianamine synthase( domain architecture ID 10010987)
nicotianamine synthase produces the polyamine nicotianamine from 3 molecules of S-adenosyl-L-methionine
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| PLN03075 | PLN03075 | nicotianamine synthase; Provisional |
1-298 | 0e+00 | |||||
nicotianamine synthase; Provisional : Pssm-ID: 178624 Cd Length: 296 Bit Score: 534.25 E-value: 0e+00
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| Name | Accession | Description | Interval | E-value | |||||
| PLN03075 | PLN03075 | nicotianamine synthase; Provisional |
1-298 | 0e+00 | |||||
nicotianamine synthase; Provisional Pssm-ID: 178624 Cd Length: 296 Bit Score: 534.25 E-value: 0e+00
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| NAS | pfam03059 | Nicotianamine synthase protein; Nicotianamine synthase EC:2.5.1.43 catalyzes the trimerization ... |
7-278 | 1.14e-159 | |||||
Nicotianamine synthase protein; Nicotianamine synthase EC:2.5.1.43 catalyzes the trimerization of S-adenosylmethionine to yield one molecule of nicotianamine. Nicotianamine has an important role in plant iron uptake mechanisms. Plants adopt two strategies (termed I and II) of iron acquisition. Strategy I is adopted by all higher plants except graminaceous plants, which adopt strategy II. In strategy I plants, the role of nicotianamine is not fully determined: possible roles include the formation of more stable complexes with ferrous than with ferric ion, which might serve as a sensor of the physiological status of iron within a plant, or which might be involved in the transport of iron. In strategy II (graminaceous) plants, nicotianamine is the key intermediate (and nicotianamine synthase the key enzyme) in the synthesis of the mugineic family (the only known family in plants) of phytosiderophores. Phytosiderophores are iron chelators whose secretion by the roots is greatly increased in instances of iron deficiency. The 3D structures of five example NAS from Methanothermobacter thermautotrophicus reveal the monomer to consist of a five-helical bundle N-terminal domain on top of a classic Rossmann fold C-terminal domain. The N-terminal domain is unique to the NAS family, whereas the C-terminal domain is homologous to the class I family of SAM-dependent methyltransferases. An active site is created at the interface of the two domains, at the rim of a large cavity that corresponds to the nucleotide binding site such as is found in other proteins adopting a Rossmann fold. Pssm-ID: 308600 [Multi-domain] Cd Length: 276 Bit Score: 446.82 E-value: 1.14e-159
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| GH4_alpha_glucosidase_galactosidase | cd05297 | Glycoside Hydrolases Family 4; Alpha-glucosidases and alpha-galactosidases; Glucosidases ... |
128-223 | 4.00e-03 | |||||
Glycoside Hydrolases Family 4; Alpha-glucosidases and alpha-galactosidases; Glucosidases cleave glycosidic bonds to release glucose from oligosaccharides. Alpha-glucosidases and alpha-galactosidases release alpha-D-glucose and alpha-D-galactose, respectively, via the hydrolysis of alpha-glycopyranoside bonds. Some bacteria simultaneously translocate and phosphorylate disaccharides via the phosphoenolpyruvate-dependent phosphotransferase system (PEP-PTS). After translocation, these phospho-disaccharides may be hydrolyzed by the GH4 glycoside hydrolases such as the alpha-glucosidases. Other organsisms (such as archaea and Thermotoga maritima) lack the PEP-PTS system, but have several enzymes normally associated with the PEP-PTS operon. Alpha-glucosidases and alpha-galactosidases are part of the NAD(P)-binding Rossmann fold superfamily, which includes a wide variety of protein families including the NAD(P)-binding domains of alcohol dehydrogenases, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate dehydrogenases, formate/glycerate dehydrogenases, siroheme synthases, 6-phosphogluconate dehydrogenases, aminoacid dehydrogenases, repressor rex, and NAD-binding potassium channel domains, among others. Pssm-ID: 133433 [Multi-domain] Cd Length: 423 Bit Score: 38.70 E-value: 4.00e-03
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| Name | Accession | Description | Interval | E-value | |||||
| PLN03075 | PLN03075 | nicotianamine synthase; Provisional |
1-298 | 0e+00 | |||||
nicotianamine synthase; Provisional Pssm-ID: 178624 Cd Length: 296 Bit Score: 534.25 E-value: 0e+00
|
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| NAS | pfam03059 | Nicotianamine synthase protein; Nicotianamine synthase EC:2.5.1.43 catalyzes the trimerization ... |
7-278 | 1.14e-159 | |||||
Nicotianamine synthase protein; Nicotianamine synthase EC:2.5.1.43 catalyzes the trimerization of S-adenosylmethionine to yield one molecule of nicotianamine. Nicotianamine has an important role in plant iron uptake mechanisms. Plants adopt two strategies (termed I and II) of iron acquisition. Strategy I is adopted by all higher plants except graminaceous plants, which adopt strategy II. In strategy I plants, the role of nicotianamine is not fully determined: possible roles include the formation of more stable complexes with ferrous than with ferric ion, which might serve as a sensor of the physiological status of iron within a plant, or which might be involved in the transport of iron. In strategy II (graminaceous) plants, nicotianamine is the key intermediate (and nicotianamine synthase the key enzyme) in the synthesis of the mugineic family (the only known family in plants) of phytosiderophores. Phytosiderophores are iron chelators whose secretion by the roots is greatly increased in instances of iron deficiency. The 3D structures of five example NAS from Methanothermobacter thermautotrophicus reveal the monomer to consist of a five-helical bundle N-terminal domain on top of a classic Rossmann fold C-terminal domain. The N-terminal domain is unique to the NAS family, whereas the C-terminal domain is homologous to the class I family of SAM-dependent methyltransferases. An active site is created at the interface of the two domains, at the rim of a large cavity that corresponds to the nucleotide binding site such as is found in other proteins adopting a Rossmann fold. Pssm-ID: 308600 [Multi-domain] Cd Length: 276 Bit Score: 446.82 E-value: 1.14e-159
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| GH4_alpha_glucosidase_galactosidase | cd05297 | Glycoside Hydrolases Family 4; Alpha-glucosidases and alpha-galactosidases; Glucosidases ... |
128-223 | 4.00e-03 | |||||
Glycoside Hydrolases Family 4; Alpha-glucosidases and alpha-galactosidases; Glucosidases cleave glycosidic bonds to release glucose from oligosaccharides. Alpha-glucosidases and alpha-galactosidases release alpha-D-glucose and alpha-D-galactose, respectively, via the hydrolysis of alpha-glycopyranoside bonds. Some bacteria simultaneously translocate and phosphorylate disaccharides via the phosphoenolpyruvate-dependent phosphotransferase system (PEP-PTS). After translocation, these phospho-disaccharides may be hydrolyzed by the GH4 glycoside hydrolases such as the alpha-glucosidases. Other organsisms (such as archaea and Thermotoga maritima) lack the PEP-PTS system, but have several enzymes normally associated with the PEP-PTS operon. Alpha-glucosidases and alpha-galactosidases are part of the NAD(P)-binding Rossmann fold superfamily, which includes a wide variety of protein families including the NAD(P)-binding domains of alcohol dehydrogenases, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate dehydrogenases, formate/glycerate dehydrogenases, siroheme synthases, 6-phosphogluconate dehydrogenases, aminoacid dehydrogenases, repressor rex, and NAD-binding potassium channel domains, among others. Pssm-ID: 133433 [Multi-domain] Cd Length: 423 Bit Score: 38.70 E-value: 4.00e-03
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| Blast search parameters | ||||
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