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EC Tree
IUBMB Comments ABC-type (ATP-binding cassette-type) transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. A bacterial enzyme that interacts with an extracytoplasmic substrate binding protein and functions to import methionine. The enzyme from Escherichia coli K-12 mediates the high affinity transport of both L- and D-methionine, as well as methionine-S-oxide and N-acetyl-DL-methionine.
The enzyme appears in viruses and cellular organisms
Reaction Schemes
+
+
L-methionine-[methionine-binding protein][side 1]
=
+
+
+
[methionine-binding protein][side 1]
+
+
D-methionine-[methionine-binding protein][side 1]
=
+
+
+
[methionine-binding protein][side 1]
Synonyms
metni, metniq, methionine abc transporter, methionine uptake transporter, methionine importer, d-methionine transporter,
more
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D-methionine transporter
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methionine ABC transporter
methionine ATP binding cassette transporter
methionine transporting ATPase
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methionine uptake transporter
metI
transmembrane subunit
MetNIQ ABC transporter
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metD
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metD
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MetD is an ABC transporter with Abc the ATPase, YaeE the permease, and YaeC the likely substrate binding protein
methionine ABC transporter
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methionine ABC transporter
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methionine ATP binding cassette transporter
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methionine ATP binding cassette transporter
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methionine uptake transporter
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methionine uptake transporter
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metN
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MetNI
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metNIQ
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + H2O + D-methionine-[methionine-binding protein][side 1] = ADP + phosphate + D-methionine[side 2] + [methionine-binding protein][side 1]
(2)
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ATP + H2O + L-methionine-[methionine-binding protein][side 1] = ADP + phosphate + L-methionine[side 2] + [methionine-binding protein][side 1]
(1)
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ATP phosphohydrolase (ABC-type, methionine-importing)
ABC-type (ATP-binding cassette-type) transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. A bacterial enzyme that interacts with an extracytoplasmic substrate binding protein and functions to import methionine. The enzyme from Escherichia coli K-12 mediates the high affinity transport of both L- and D-methionine, as well as methionine-S-oxide and N-acetyl-DL-methionine.
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ATP + H2O + alpha-methyl methionine-[methionine-binding protein][side 1]
ADP + phosphate + alpha-methyl methionine[side 2] + [methionine-binding protein][side 1]
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?
ATP + H2O + D-methionine-[methionine-binding protein][side 1]
ADP + phosphate + D-methionine[side 2] + [methionine-binding protein][side 1]
ATP + H2O + D-selenomethionine-[methionine-binding protein][side 1]
ADP + phosphate + D-selenomethionine[side 2] + [methionine-binding protein][side 1]
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-
-
?
ATP + H2O + L-methionine-[methionine-binding protein][side 1]
ADP + phosphate + L-methionine[side 2] + [methionine-binding protein][side 1]
ATP + H2O + L-selenomethionine-[methionine-binding protein][side 1]
ADP + phosphate + L-selenomethionine[side 2] + [methionine-binding protein][side 1]
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?
ATP + H2O + D-methionine-[methionine-binding protein][side 1]
ADP + phosphate + D-methionine[side 2] + [methionine-binding protein][side 1]
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?
ATP + H2O + D-methionine-[methionine-binding protein][side 1]
ADP + phosphate + D-methionine[side 2] + [methionine-binding protein][side 1]
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?
ATP + H2O + D-methionine-[methionine-binding protein][side 1]
ADP + phosphate + D-methionine[side 2] + [methionine-binding protein][side 1]
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?
ATP + H2O + D-methionine-[methionine-binding protein][side 1]
ADP + phosphate + D-methionine[side 2] + [methionine-binding protein][side 1]
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?
ATP + H2O + D-methionine-[methionine-binding protein][side 1]
ADP + phosphate + D-methionine[side 2] + [methionine-binding protein][side 1]
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?
ATP + H2O + L-methionine-[methionine-binding protein][side 1]
ADP + phosphate + L-methionine[side 2] + [methionine-binding protein][side 1]
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?
ATP + H2O + L-methionine-[methionine-binding protein][side 1]
ADP + phosphate + L-methionine[side 2] + [methionine-binding protein][side 1]
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?
ATP + H2O + L-methionine-[methionine-binding protein][side 1]
ADP + phosphate + L-methionine[side 2] + [methionine-binding protein][side 1]
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?
ATP + H2O + L-methionine-[methionine-binding protein][side 1]
ADP + phosphate + L-methionine[side 2] + [methionine-binding protein][side 1]
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?
ATP + H2O + L-methionine-[methionine-binding protein][side 1]
ADP + phosphate + L-methionine[side 2] + [methionine-binding protein][side 1]
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?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + H2O + D-methionine-[methionine-binding protein][side 1]
ADP + phosphate + D-methionine[side 2] + [methionine-binding protein][side 1]
ATP + H2O + L-methionine-[methionine-binding protein][side 1]
ADP + phosphate + L-methionine[side 2] + [methionine-binding protein][side 1]
ATP + H2O + D-methionine-[methionine-binding protein][side 1]
ADP + phosphate + D-methionine[side 2] + [methionine-binding protein][side 1]
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?
ATP + H2O + D-methionine-[methionine-binding protein][side 1]
ADP + phosphate + D-methionine[side 2] + [methionine-binding protein][side 1]
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?
ATP + H2O + D-methionine-[methionine-binding protein][side 1]
ADP + phosphate + D-methionine[side 2] + [methionine-binding protein][side 1]
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?
ATP + H2O + D-methionine-[methionine-binding protein][side 1]
ADP + phosphate + D-methionine[side 2] + [methionine-binding protein][side 1]
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?
ATP + H2O + D-methionine-[methionine-binding protein][side 1]
ADP + phosphate + D-methionine[side 2] + [methionine-binding protein][side 1]
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?
ATP + H2O + L-methionine-[methionine-binding protein][side 1]
ADP + phosphate + L-methionine[side 2] + [methionine-binding protein][side 1]
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?
ATP + H2O + L-methionine-[methionine-binding protein][side 1]
ADP + phosphate + L-methionine[side 2] + [methionine-binding protein][side 1]
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?
ATP + H2O + L-methionine-[methionine-binding protein][side 1]
ADP + phosphate + L-methionine[side 2] + [methionine-binding protein][side 1]
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ATP + H2O + L-methionine-[methionine-binding protein][side 1]
ADP + phosphate + L-methionine[side 2] + [methionine-binding protein][side 1]
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?
ATP + H2O + L-methionine-[methionine-binding protein][side 1]
ADP + phosphate + L-methionine[side 2] + [methionine-binding protein][side 1]
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?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Mg2+
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required
Mg2+
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required for activity
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ADP
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competitive inhibitor
D-alanine
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94% residual activity at 5 mM with L-methionine as substrate
D-leucine
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98% residual activity at 5 mM with L-methionine as substrate, 90% residual activity at 50 mM with D-methionine as substrate
D-methionine
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92% residual activity at 5 mM with L-methionine as substrate, 23% residual activity at 50 mM with D-methionine as substrate
D-serine
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86% residual activity at 5 mM with L-methionine as substrate
D-threonine
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94% residual activity at 5 mM with L-methionine as substrate
L-alanine
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91% residual activity at 5 mM with L-methionine as substrate, 95% residual activity at 50 mM with D-methionine as substrate
L-leucine
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84% residual activity at 5 mM with L-methionine as substrate, 94% residual activity at 50 mM with D-methionine as substrate
L-threonine
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89% residual activity at 5 mM with L-methionine as substrate
L-valine
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77% residual activity at 5 mM with L-methionine as substrate, 81% residual activity at 50 mM with D-methionine as substrate
N-formyl-L-methionine
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39% residual activity at 5 mM with L-methionine as substrate, 25% residual activity at 50 mM with D-methionine as substrate
L-methionine
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7% residual activity at 5 mM with L-methionine as substrate, 12% residual activity at 50 mM with D-methionine as substrate
L-methionine
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noncompetitive inhibitor of enzyme ATPase activity. The uptake of external methionine is repressed by the level of the internal L-methionine pool (transinhibition)
L-methionine
inhibits the ATPase activity of the enzyme
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D-alanine
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106% activity at 50 mM with D-methionine as substrate
D-serine
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118% activity at 50 mM with D-methionine as substrate
D-threonine
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115% activity at 50 mM with D-methionine as substrate
L-serine
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121% activity at 5 mM with L-methionine as substrate, 114% activity at 50 mM with D-methionine as substrate
L-threonine
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120% activity at 50 mM with D-methionine as substrate
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.33
ATP
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at pH 7.5 and 33°C
0.0014 - 0.0074
D-selenomethionine-[methionine-binding protein][side 1]
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0.0014
D-selenomethionine-[methionine-binding protein][side 1]
mutant enzyme N295A/M163A, at pH 6.5 and 37°C
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0.0017
D-selenomethionine-[methionine-binding protein][side 1]
mutant enzyme N295A, at pH 6.5 and 37°C
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0.0018
D-selenomethionine-[methionine-binding protein][side 1]
wild type enzyme, at pH 6.5 and 37°C
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0.0041
D-selenomethionine-[methionine-binding protein][side 1]
mutant enzyme N229A/Y160A, at pH 6.5 and 37°C
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0.0048
D-selenomethionine-[methionine-binding protein][side 1]
mutant enzyme N295A/N229A, at pH 6.5 and 37°C
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0.0074
D-selenomethionine-[methionine-binding protein][side 1]
mutant enzyme N229A, at pH 6.5 and 37°C
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0.041
ADP
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at pH 7.5 and 33°C
0.041
L-methionine
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at pH 7.5 and 33°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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brenda
metN and metI subunits
UniProt
brenda
metN ATPase and metI permease components
UniProt
brenda
metN subunit and metI subunit
UniProt
brenda
subunits metN and metI
UniProt
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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brenda
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brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
metabolism
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the enzyme regulates intracellular methionine concentrations
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ATPgammaS-bound MetNIQ complex in the outwardfacing conformation with the N229A apo MetQ variant, hanging drop vapor diffusion method, using 0.1 M Mes, pH 6.0, and 22% (w/v) PEG 400
hanging drop vapor diffusion method, using 28-32% (w/v) PEG 400, 0.05 M Li2SO4, 0.2 M (NH4)2HPO4, 0.05-0.15 M (NH2)2SO4, and 0.1 M sodium citrate pH 4.2-4.5
mutant enzyme E166Q in inward facing conformations, purified in cyclohexyl-pentyl-beta-D-maltoside and n-decyl-beta-D-maltopyranoside, sitting drop vapor diffusion method, using 25% (w/v) polyethylene glycol 400, 0.1 M Tris, pH 7.3
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N295A
the mutation results in a higher maximal uptake rate with no change in Km value compared to the wild type enzyme
N295A/M163A
the mutations result in a lower maximal uptake rate with decreased Km value compared to the wild type enzyme
N295A/N229A
the mutations result in a higher maximal uptake rate with increased Km value compared to the wild type enzyme
E166Q
inactive
E166Q
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ATPase-deficient mutant
N229A
the substrate-binding deficient variant of the cognate binding protein MetQ supports high transport activity toward D-selenomethionine
N229A
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the variant of the binding protein MetQ disrupts methionine binding
N295A/Y160A
inactive
N295A/Y160A
the mutations result in a higher maximal uptake rate with increased Km value compared to the wild type enzyme
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HisTrap column chromatography and Superdex S200 gel filtration
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Ni-Sepharose column chromatography
Ni-Sepharose column chromatography and gel filtration
Ni-Sepharose column chromatography
Ni-Sepharose column chromatography
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expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli BL21-Gold (DE3) cells
expressed in Escherichia coli BL21-Gold (lambdaDE3) cells
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expressed in Escherichia coli BL21-Gold (lambdaDE3)cells
expressed in Escherichia coli JM109 cells
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expressed in Escherichia coli BL21-Gold (lambdaDE3)cells
expressed in Escherichia coli BL21-Gold (lambdaDE3)cells
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
enzyme expression decreased about 3fold upon the addition of L-methionine to the medium and about 2fold when the metJ gene is present in multicopy. When both L-methionine is added and metJ is present in multicopy, the enzyme expression decreases about 12fold
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MetJ is the pleiotropic methionine repressor protein that negatively control expression of the operon encoding the ABC-type methionine uptake system
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Zhang, Z.; Feige, J.N.; Chang, A.B.; Anderson, I.J.; Brodianski, V.M.; Vitreschak, A.G.; Gelfand, M.S.; Saier, M.H.
A transporter of Escherichia coli specific for L- and D-methionine is the prototype for a new family within the ABC superfamily
Arch. Microbiol.
180
88-100
2003
Escherichia coli
brenda
Nguyen, P.T.; Li, Q.W.; Kadaba, N.S.; Lai, J.Y.; Yang, J.G.; Rees, D.C.
The contribution of methionine to the stability of the Escherichia coli MetNIQ ABC transporter-substrate binding protein complex
Biol. Chem.
396
1127-1134
2015
Escherichia coli
brenda
Gal, J.; Szvetnik, A.; Schnell, R.; Kalman, M.
The metD D-methionine transporter locus of Escherichia coli is an ABC transporter gene cluster
J. Bacteriol.
184
4930-4932
2002
Escherichia coli
brenda
Merlin, C.; Gardiner, G.; Durand, S.; Masters, M.
The Escherichia coli metD locus encodes an ABC transporter which includes Abc (MetN), YaeE (MetI), and YaeC (MetQ)
J. Bacteriol.
184
5513-5517
2002
Escherichia coli
brenda
Yang, J.G.; Rees, D.C.
The allosteric regulatory mechanism of the Escherichia coli MetNI methionine ATP binding cassette (ABC) transporter
J. Biol. Chem.
290
9135-9140
2015
Escherichia coli
brenda
Yang, Z.; Niu, X.; Zhang, H.; Wang, S.; Zhao, X.; Huang, X.
Conformational changes in MetNI Steered molecular dynamic studies of the methionine ABC transporter with and without substrates
Mol. Simul.
41
613-621
2015
Escherichia coli (P30750 and P31547)
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brenda
Nguyen, P.T.; Lai, J.Y.; Lee, A.T.; Kaiser, J.T.; Rees, D.C.
Noncanonical role for the binding protein in substrate uptake by the MetNI methionine ATP binding cassette (ABC) transporter
Proc. Natl. Acad. Sci. USA
115
10596-10604
2018
Escherichia coli (P30750 and P31547), Escherichia coli
brenda
Johnson, E.; Nguyen, P.T.; Yeates, T.O.; Rees, D.C.
Inward facing conformations of the MetNI methionine ABC transporter Implications for the mechanism of transinhibition
Protein Sci.
21
84-96
2012
Escherichia coli (P30750 and P31547), Escherichia coli
brenda
Kadaba, N.; Kaiser, J.; Johnson, E.; Lee, A.; Rees, D.
The high-affinity E. coli methionine ABC transporter Structure and allosteric regulation
Science
321
250-253
2008
Escherichia coli (P30750 and P31547), Escherichia coli
brenda
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