Any feedback?
Information on EC 7.2.2.14 - P-type Mg2+ transporter
for references in articles please use BRENDA:EC7.2.2.14Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
7.2.2.14 P-type Mg2+ transporterIUBMB 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.
Specify your search results
Word Map
- 7.2.2.14
- na+
- atpases
- triphosphatase
- mg2+-atpase
-
sarcoplasmic
-
ca2+-stimulated
-
submitochondrial
- ouabain
-
sarcolemmal
- myofibrillar
-
amelogenesis
-
hypomagnesemia
- medicine
- imperfecta
- actomyosin
-
cone-rode
-
actin-activated
-
oligomycin-insensitive
-
ouabain-sensitive
- dicyclohexylcarbodiimide
-
atp-driven
- ecto-atpase
- n,n'-dicyclohexylcarbodiimide
-
melastatin
-
3.6.1.3
- synthesis
- biotechnology
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
adenosine 5'-triphosphatase
-
-
-
-
adenosine triphosphatase
-
-
-
-
ATP hydrolase
-
-
-
-
ATP phosphohydrolase
-
-
-
-
ATPase
-
-
-
-
complex V (mitochondrial electron transport)
-
-
-
-
additional information
additional information
the enzyme belongs to the 2-TM-GxN family of Mg2+ transporters
additional information
the enzyme belongs to the CorA-Alr1-Mrs2 superfamily
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + H2O + Mg2+[side 1] = ADP + phosphate + Mg2+[side 2]
Mg2+ transport involves first the binding of the fully hydrated ion to an extracellular binding loop connecting the transmembrane domain, passage through the membrane, not involving electrostatic interactions but two cytsolic domains, one with extremely high positive charges and the other with negative charge helping to control the Mg2+ flux in concert with an intracellular Mg2+ bound between the domains of each monomer, transport mechanism, overview
ATP + H2O + Mg2+[side 1] = ADP + phosphate + Mg2+[side 2]
Mg2+ transport mechanism, structure-function relationship, overview
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
transmembrane transport
-
-
-
-
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
9000-83-3
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + H2O + Mg2+/out
ADP + phosphate + Mg2+/in
-
-
-
?
ATP + H2O + Mg2+/out
ADP + phosphate + Mg2+/in
CorA contains an unusually long ion pore putatively gated by hydrophobic residues near the intracellular end and by universally conserved asparagine residues at the periplasmic entrance, structure-function relationships and gating mechanisms in the CorA Mg2+ transport system, the intracellular funnel domain constitutes an allosteric regulatory module that can be engineered to promote an activated or closed state, involvement of the alpha5 and alpha6 helices in CorA function, overview
-
-
?
ATP + H2O + Mg2+/out
ADP + phosphate + Mg2+/in
One metal binds near the universally conserved GMN motif, apparently stabilized within the transmembrane region discriminating between the size and preferred coordination geometry of hydrated substrates. CorA achieves specificity by requiring the sequential dehydration of substrates. Ten metal sites are located within the cytoplasmic funnel domain and linked to long extensions of the pore helices regulating the transport status of CorA, this region is an intrinsic divalent cation sensor functioning as a Mg2+-specific homeostatic molecular switch, overview
-
-
?
additional information
?
-
CorA does not contain an ATP binding site and acts as a Mg2+ channel probably driven by the inward electrochemical Mg2+ potential
-
-
?
additional information
?
-
CorA is selective for magnesium ions over calcium ions with a 100fold greater uptake rate
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). CORA_THEMA
Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
351
0
41446
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
42000
5 * 42000, about, SDS-PAGE, a funnel-shaped homopentamer with two transmembrane helices per monomer, the large cytosolic domain forms the funnel, overview
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pentamer
additional information
pentamer
5 * 42000, about, SDS-PAGE, a funnel-shaped homopentamer with two transmembrane helices per monomer, the large cytosolic domain forms the funnel, overview
additional information
CorA contains an unusually long ion pore putatively gated by hydrophobic residues near the intracellular end and by universally conserved asparagine residues at the periplasmic entrance
additional information
secondary structure determination and analysis
additional information
structural basis for Mg2+ homeostasis and the CorA translocation cycle, open state model and two-state model, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure analysis from PDB ID BBJ2 at 3.9 A resolution for the whole enzyme, and at 1.8 A resolution for the soluble domain, overview
free wild-type CorA, CorA1-351, and SeMet-AfCorA1-263, in complex with several different metal ions, 15 mg/ml purified CorA1-351 in 20 mM Tris pH 8.0, 100 mM NaCl, 1 mM TCEP, with or without 0.026% n-dodecyl-beta-D-maltoside, with precipitant vapor-diffusion over 20% PEG 400, 0.2 M CaCl2, 0.1 M HEPES, pH 7.0, 40 mg/ml native and SeMet-AfCorA1-263 from 1.3 M ammonium sulfate, 10 mM CoCl2, 0.1 M HEPES, pH 7.4, X-ray diffraction structure determination and analysis at 3.7 A resolution
recombinant enzyme, purification omits the isolation and subsequent solubilization of the membrane fraction
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D253F
site-directed mutagenesis, structural alterations and Mg2+ transport in comparison to the wild-type enzyme, overview
D253K
site-directed mutagenesis, structural alterations and Mg2+ transport in comparison to the wild-type enzyme, overview
D253W
site-directed mutagenesis, structural alterations and Mg2+ transport in comparison to the wild-type enzyme, overview
E206R
site-directed mutagenesis, structural alterations and Mg2+ transport in comparison to the wild-type enzyme, overview
E316K
site-directed mutagenesis, structural alterations and Mg2+ transport in comparison to the wild-type enzyme, overview
E316K/E320A
site-directed mutagenesis, with mutation of Gly4alpha5alpha6, structural alterations and Mg2+ transport in comparison to the wild-type enzyme, overview
E320K
site-directed mutagenesis, structural alterations and Mg2+ transport in comparison to the wild-type enzyme, overview
P303I
site-directed mutagenesis, structural alterations and Mg2+ transport in comparison to the wild-type enzyme, overview
V194E
site-directed mutagenesis, structural alterations and Mg2+ transport in comparison to the wild-type enzyme, overview
V194E/E206R
site-directed mutagenesis, structural alterations and Mg2+ transport in comparison to the wild-type enzyme, overview
additional information
additional information
deletion mutant Gly4alpha5alpha6, site-directed mutagenesis, structural alterations and Mg2+ transport in comparison to the wild-type enzyme, overview
additional information
mutation of residues near L294/M291 alters the transport properties of CorA
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme, purification omits the isolation and subsequent solubilization of the membrane fraction
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21 by nickel affinity chromatography, cleavage of the His-tag, and gel filtration to homogeneity
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21, complementation of Salmonella typhimurium MM281, a strain devoid of all genomic Mg2+ transport systems
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
reconstitution of the purified recombinant enzyme in phosphatidylcholine liposomes, overview
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Payandeh, J.; Pai, E.F.
Crystallization and preliminary X-ray diffraction analysis of the magnesium transporter CorA
Acta Crystallogr. Sect. F
62
148-152
2006
Archaeoglobus fulgidus (O29487), Archaeoglobus fulgidus, Thermotoga maritima (Q9WZ31), Thermotoga maritima
Payandeh, J.; Pai, E.F.
A structural basis for Mg2+ homeostasis and the CorA translocation cycle
EMBO J.
25
3762-3773
2006
Thermotoga maritima (Q9WZ31)
Maguire, M.E.
Magnesium transporters: properties, regulation and structure
Front. Biosci.
11
3149-3163
2006
Aeromonas hydrophila, Arabidopsis thaliana, Cytobacillus firmus, Cytobacillus firmus OF4, Escherichia coli, Methanocaldococcus jannaschii (Q58439), Methanosarcina sp., Methanothermobacter sp., Mycobacterium tuberculosis, Providencia stuartii, Salmonella enterica subsp. enterica serovar Typhimurium, Thermotoga maritima (Q9WZ31)
Payandeh, J.; Li, C.; Ramjeesingh, M.; Poduch, E.; Bear, C.E.; Pai, E.F.
Probing structure-function relationships and gating mechanisms in the CorA Mg2+ transport system
J. Biol. Chem.
283
11721-11733
2008
Thermotoga maritima (Q9WZ31)
Papp-Wallace, K.M.; Maguire, M.E.
Bacterial homologs of eukaryotic membrane proteins: the 2-TM-GxN family of Mg2+ transporters (Review)
Mol. Membr. Biol.
24
351-356
2007
Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium, Saccharomyces cerevisiae (P43553), Saccharomyces cerevisiae (Q02783), Saccharomyces cerevisiae (Q08269), Thermotoga maritima (Q9WZ31)
EXTERNAL LINKS (specific for EC-Number 7.2.2.14)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
