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Information on EC 7.2.2.14 - P-type Mg2+ transporter

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EC Tree
IUBMB Comments
A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. A bacterial enzyme that imports Mg2+ with, rather than against, the Mg2+ electrochemical gradient. The enzyme is also involved in Ni2+ import.
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This record set is specific for:
UNIPROT: Q5SMG8
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Word Map
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
mg2+ atpase, mg2+-dependent atpase, magt1, slc41a1, oligomycin-sensitive atpase, magnesium transporter, cnnm4, mg2+ transporter, mrs2p, magnesium transporter subtype 1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+ transporter
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adenosine 5'-triphosphatase
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adenosine triphosphatase
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ATP hydrolase
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ATP phosphohydrolase
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ATPase
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complex V (mitochondrial electron transport)
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
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transmembrane transport
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SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (P-type, Mg2+-importing)
A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. A bacterial enzyme that imports Mg2+ with, rather than against, the Mg2+ electrochemical gradient. The enzyme is also involved in Ni2+ import.
CAS REGISTRY NUMBER
COMMENTARY hide
9000-83-3
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + H2O + Mg2+/out
ADP + phosphate + Mg2+/in
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + H2O + Mg2+/out
ADP + phosphate + Mg2+/in
show the reaction diagram
Mg21 homeostasis mechanism model, overview
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?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene mgtE
SwissProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
the transmembrane helices are connected by 5 loops, structure, overview
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
MGTE_THET8
Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
450
0
50078
Swiss-Prot
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
selenomethionine-labeled full-length enzyme and soluble cytosolic domain in presence and absence of Mg2+, 10 mg/ml full-length protein with 0.1% dodecylmaltoside, by vapour diffusion over 32-34% 2-methyl-2,4-pentanediol, 40 mM magnesium acetate, and 100 mM MES, pH 6.0, cytosolic domain with bound Mg2+ by vapour diffusion over solutions containing 18-22% PEG 400, 0.2M MgCl2, and 0.1M HEPES, pH 7.4, or cytosolic domain in the absence of Mg2+ in 20% PEG 3350, 0.2 M ammonium acetate, and 0.5% octyl-beta-D-glucopyranoside, X-ray diffraction structure determination at 2.3-3.9 A resolution, multiple anomaleous dispersion method
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant N-terminally His-tagged cytosolic domain by nickel affinity chromatography, tag cleavage by thrombin, anion exchange chromatography and gel filtration, recombinant N-terminally His-tagged full-length MgtE from Escherichia coli strain C41 (DE3) by nickel affinity chromatography and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene mgtE, overexpression of N-terminally His-tagged full-length enzyme and cytosolic domain in Escherichia coli strain C41 (DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hattori, M.; Tanaka, Y.; Fukai, S.; Ishitani, R.; Nureki, O.
Crystal structure of the MgtE Mg2+ transporter
Nature
448
1072-1075
2007
Thermus thermophilus (Q5SMG8), Thermus thermophilus
Manually annotated by BRENDA team