Any feedback?
Information on EC 7.2.2.10 - P-type Ca2+ transporter and Organism(s) Arabidopsis thaliana and UniProt Accession P92939
for references in articles please use BRENDA:EC7.2.2.10Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
7.2.2.10 P-type Ca2+ transporterIUBMB Comments
A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. This enzyme family comprises three types of Ca2+-transporting enzymes that are found in the plasma membrane, the sarcoplasmic reticulum, in yeast, and in some bacteria. The enzymes from plasma membrane and from yeast have been shown to transport one ion per ATP hydrolysed whereas those from the sarcoplasmic reticulum transport two ions per ATP hydrolysed. In muscle cells Ca2+ is transported from the cytosol (side 1) into the sarcoplasmic reticulum (side 2).
Specify your search results
Word Map
- 7.2.2.10
- cardiac
- thapsigargin
-
contractile
- ventricular
- phospholamban
- myocardial
- cardiomyocytes
- calmodulin
-
ryanodine
- myocytes
- na+
- myosin
-
pmcas
- atpases
- hypertrophy
-
blocker
-
cyclopiazonic
- inositol
-
diastolic
- caffeine
-
ca2+-free
-
fura-2
-
l-type
- vanadate
-
extrusion
- plb
- overload
- phosphoenzyme
-
systolic
- nifedipine
- cpa
-
excitation-contraction
- ouabain
-
store-operated
-
1,4,5-trisphosphate
-
ca2+-binding
-
calmodulin-dependent
-
twitch
- na+-k+-atpase
-
slow-twitch
-
ca2+-sensitive
- na,k-atpase
-
refilling
-
inotropic
- myofibrillar
-
k+-atpase
-
fast-twitch
-
ca2+-induced
- medicine
- insp3
-
actin-activated
- biotechnology
- pharmacology
- agriculture
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
serca, ca2+-atpase, serca2a, ca2+ pump, serca2, ca-atpase, calcium pump, ca2+ atpase, serca1, serca2b, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ACA8
ATP-dependent Ca2+ pump PMR1
-
-
-
-
ATPase 2C1
-
-
-
-
Ca2+ ATPase
-
-
-
-
Ca2+-ATPase, isoform 10
-
-
-
-
Ca2+-ATPase, isoform 11
-
-
-
-
Ca2+-ATPase, isoform 12
-
-
-
-
Ca2+-ATPase, isoform 13
-
-
-
-
Ca2+-pumping ATPase
Ca2+-transporting ATPase
-
-
-
-
calcium pump
-
-
-
-
Calcium-transporting ATPase sarcoplasmic reticulum type, fast twitch skeletal muscle isoform
-
-
-
-
Calcium-transporting ATPase sarcoplasmic reticulum type, slow twitch skeletal muscle isoform
-
-
-
-
ChkSERCA3
-
-
-
-
endoplasmic reticulum class 1/2 Ca(2+) ATPase
-
-
-
-
Golgi Ca2+-ATPase
-
-
-
-
HUSSY-28
-
-
-
-
P-type calcium ATPase
-
-
-
-
phosphatase, adenosine tri
-
-
-
-
plasma membrane Ca-ATPase
-
-
-
-
PMCA1
-
-
-
-
PMCA2
-
-
-
-
PMCA3
-
-
-
-
PMCA4
-
-
-
-
sarco(endo)plasmic reticulum Ca2+-ATPase
-
-
-
-
sarcoplasmic reticulum ATPase
-
-
-
-
Secretory pathway Ca2+ transporting ATPase
-
-
-
-
SERCA
-
-
-
-
SERCA1
-
-
-
-
SERCA2
-
-
-
-
SERCA3
-
-
-
-
Vacuolar Ca2+-ATPase
-
-
-
-
additional information
Ca2+-pumping ATPase
-
-
-
-
additional information
-
the enzyme belongs to the P2B subfamily of P-type ATPases
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (P-type, Ca2+-transporting)
A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. This enzyme family comprises three types of Ca2+-transporting enzymes that are found in the plasma membrane, the sarcoplasmic reticulum, in yeast, and in some bacteria. The enzymes from plasma membrane and from yeast have been shown to transport one ion per ATP hydrolysed whereas those from the sarcoplasmic reticulum transport two ions per ATP hydrolysed. In muscle cells Ca2+ is transported from the cytosol (side 1) into the sarcoplasmic reticulum (side 2).
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 + Ca2+/cis
ADP + phosphate + Ca2+/trans
-
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
-
-
-
?
ATP + H2O + Ca2+/in
ADP + phosphate + Ca2+/out
-
plasma-membrane Ca2+-ATPase is a calcium pump that exports Ca2+ from the cytosol to the extracellular environment of eukaryotic cells and thus maintain overall Ca2+ homoeostasis and provide local control of intracellular Ca2+ signalling
-
-
?
additional information
?
-
the Arabidopsis thaliana endoplasmic reticulum-localized Ca2+-ATPase, ECA1, with homology to PMR1, can also transport Mn2+. Molecular determinants of the Mn2+ specificity of transport proteins
-
-
-
additional information
?
-
isoform ECA3 function cannot be replaced by an endoplasmic reticulum-associated isoform ECA1, ECA3 is also important for the detoxification of excess Mn2+, isoform ECA3 is a distinct Ca2+/Mn2+ pump critical for Ca2+-enhanced root growth
-
-
?
additional information
?
-
isoform ECA3 function cannot be replaced by an endoplasmic reticulum-associated isoform ECA1, ECA3 is also important for the detoxification of excess Mn2+, isoform ECA3 is a distinct Ca2+/Mn2+ pump critical for Ca2+-enhanced root growth
-
-
?
additional information
?
-
isoform ECA3 function cannot be replaced by an endoplasmic reticulum-associated isoform ECA1, ECA3 is also important for the detoxification of excess Mn2+, isoform ECA3 is a distinct Ca2+/Mn2+ pump critical for Ca2+-enhanced root growth
-
-
?
additional information
?
-
isoform ECA3 function cannot be replaced by an endoplasmic reticulum-associated isoform ECA1, ECA3 is also important for the detoxification of excess Mn2+, isoform ECA3 is a distinct Ca2+/Mn2+ pump critical for Ca2+-enhanced root growth
-
-
?
additional information
?
-
-
ER-type Ca2+-ATPases show a strong preference for ATP as substrate. Conversely, auto-inhibited Ca2+-ATPases are able to use ITP or GTP as an alternative to ATP
-
-
?
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
ATP + H2O + Ca2+/in
ADP + phosphate + Ca2+/out
-
plasma-membrane Ca2+-ATPase is a calcium pump that exports Ca2+ from the cytosol to the extracellular environment of eukaryotic cells and thus maintain overall Ca2+ homoeostasis and provide local control of intracellular Ca2+ signalling
-
-
?
additional information
?
-
isoform ECA3 function cannot be replaced by an endoplasmic reticulum-associated isoform ECA1, ECA3 is also important for the detoxification of excess Mn2+, isoform ECA3 is a distinct Ca2+/Mn2+ pump critical for Ca2+-enhanced root growth
-
-
?
additional information
?
-
isoform ECA3 function cannot be replaced by an endoplasmic reticulum-associated isoform ECA1, ECA3 is also important for the detoxification of excess Mn2+, isoform ECA3 is a distinct Ca2+/Mn2+ pump critical for Ca2+-enhanced root growth
-
-
?
additional information
?
-
isoform ECA3 function cannot be replaced by an endoplasmic reticulum-associated isoform ECA1, ECA3 is also important for the detoxification of excess Mn2+, isoform ECA3 is a distinct Ca2+/Mn2+ pump critical for Ca2+-enhanced root growth
-
-
?
additional information
?
-
isoform ECA3 function cannot be replaced by an endoplasmic reticulum-associated isoform ECA1, ECA3 is also important for the detoxification of excess Mn2+, isoform ECA3 is a distinct Ca2+/Mn2+ pump critical for Ca2+-enhanced root growth
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Mn2+
-
ER-type Ca2+-ATPases can transport, beside Ca2+, also Mn2+ and Zn2+ ions
Zn2+
-
ER-type Ca2+-ATPases can transport, beside Ca2+, also Mn2+ and Zn2+ ions
Ca2+
-
in the resting state, the plant plasma-membrane Ca2+-ATPase is autoinhibited by binding of its N-terminal tail to two major intracellular loops. Activation requires the binding of calcium-bound calmodulin to this tail and a conformational change that displaces the autoinhibitory tail from the catalytic domain
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
eosin Y
-
auto-inhibited Ca2+-ATPases are particularly sensitive to inhibition by eosin Y
erythrosin B
-
auto-inhibited Ca2+-ATPases are particularly sensitive to inhibition by erythrosin B
additional information
-
in the resting state, the plant plasma-membrane Ca2+-ATPase is autoinhibited by binding of its N-terminal tail to two major intracellular loops. Activation requires the binding of calcium-bound calmodulin to this tail and a conformational change that displaces the autoinhibitory tail from the catalytic domain
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
calcium-bound calmodulin
-
in the resting state, the plant plasma-membrane Ca2+-ATPase is autoinhibited by binding of its N-terminal tail to two major intracellular loops. Activation requires the binding of calcium-bound calmodulin to this tail and a conformational change that displaces the autoinhibitory tail from the catalytic domain
-
calmodulin-like 36
CML36 interacts directly with the regulative N terminus of the Arabidopsis plasma membrane Ca2+-ATPase isoform 8 which stimulates the enzyme activity
-
phosphatidylinositol 4-monophosphate
-
433% stimulation of activity at 1 mM
additional information
-
PMCA isoform ACA8 activity is hardly affected by phosphatidylcholine or phosphatidylethanolamine
-
Calmodulin
0.001 mM calmodulin stimulates the activity of wild type enzyme by about 300%
Calmodulin
the fully auto-inhibited enzyme has a very low basal Ca2+-ATPase activity which is stimulated more than 5fold by calmodulin
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0241
recombinant wild type enzyme, in the presence of Ca2+, pH not specified in the publication, at 25°C
0.1181
recombinant wild type enzyme, in the presence of Ca2+ and 0.001 mM calmodulin, pH not specified in the publication, at 25°C
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
a T-DNA knockout of ECA1, grown on high-Mn media, displays a strong stress phenotype when compared to wild-type plants. This phenotype includes a significant reduction in fresh weight, dramatic leaf chlorosis, a significant inhibition of leaf expansion and root elongation, and a loss of root hair tip growth. The Arabidopsis IAA-leucine resistant 2 (ilr2) mutant has a slight tolerance to Mn stress. Transport characterization of microsomal membrane vesicles from ilr2 plants demonstrated a significant increase in ATP-dependent Mn2+ transport compared to wild-type plants. ILR2 might act as a regulator of Mn2+ transport, possibly acting on Mn2+ efflux from the cell mediated by either an ATPase or an ABC transporter
metabolism
several transporter gene families have been implicated in Mn2+ transport, including cation/H+ antiporters, natural resistance-associated macrophage protein (Nramp) transporters, zinc-regulated transporter/iron-regulated transporter (ZRT/IRT1)-related protein (ZIP) transporters, the cation diffusion facilitator (CDF) transporter family, and P-type ATPases
physiological function
ECA1 is originally identified as Ca2+ transporter, but has subsequently been shown to also transport Mn2+. AtECA1 is an endoplasmic reticulum (ER) Ca2+- and Mn2+-transporting P-type ATPase (see also EC 7.2.2.22). Manganese (Mn) is an essential nutrient in plants. It is of particular importance in photosynthetic organisms where a cluster of Mn atoms is required as the catalytic centre for light-induced water oxidation in photosystem II, and is required as a cofactor for a variety of enzymes, such as the Mn2+-dependent superoxide dismutase (MnSOD). Mn can be particularly toxic to plant growth and a variety of mechanisms exist to overcome such toxicity, including the conversion of the metal to a metabolically inactive compound, such as a Mn2+-chelate complex, or sequestration of the Mn2+ ion or a Mn2+-chelate complex into an internal compartment such as the vacuole. At the cellular level, Mn2+ accumulates predominantly in the vacuole and to some extent in chloroplasts, and can be associated with the cell wall fraction. Mn2+ has a critical role in the water oxidation step of photosynthesis, and the chloroplast is the second-largest sink for Mn2+ in the cell
malfunction
-
knock-out mutants of isoform ACA9 displays reduced growth of pollen tubes, with high frequency of aborted fertilization leading to a 3fold reduction in seed set. Knock-out mutants of isoforms ACA8 or ACA10 do not have an altered phenotype, with a noticeable exception: knock-out of ACA10 in a genotype containing a naturally occurring dominant allele of an unlinked gene causes altered adult vegetative development and the formation of floral clusters. Isoform ECA1 knock-out mutant is indistinguishable from the wild type, but it clearly shows reduced root growth and toxicity symptoms when exposed to 0.5 mM Mn2+. An ECA3 knock-out mutant is not more sensitive than the wild type to Mn2+ toxicity, but rather requires higher Mn2+ concentrations for growth. Both isoform ECA1 and ECA3 knock-out mutants have slightly altered Ca2+ sensitivity
physiological function
additional information
a subfamily of P-type ATPases, the P1B-ATPases, catalyse transition metal efflux in many organisms including plants, and are predicted to transport either Zn2+/Cd2+/Pb2+/Co2+ or Cu2+/Ag2+, but there is no evidence that Mn2+ is a substrate for P1B-ATPases from any organism
physiological function
-
plasma-membrane Ca2+-ATPases, PMCAs, are high-affinity calcium pumps that expel Ca2+ from eukaryotic cells to maintain overall Ca2+ homoeostasis and to provide local control of intracellular Ca2+ signalling. They are of major physiological importance, with different isoforms being essential, for example, for presynaptic and postsynaptic Ca2+ regulation in neurons, feedback signalling in the heart and sperm motility
physiological function
-
Ca2+-ATPases use the energy of ATP hydrolysis to pump Ca2+ from the cytoplasm into intracellular compartments or into the apoplast. Ca2+-ATPases play an important role in maintenance of cytoplasmic Ca2+ homeostasis. Isoform ECA3 may also play an essential role in Mn2+ nutrition. Plasma membrane-localized auto-inhibited Ca2+-ATPases are also involved in the response to pathogens, hormonal regulation, salt stress, and cold stress
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). ECA1_ARATH
1061
8
116366
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant complex between calmodulin and the regulatory domain of the plasma-membrane Ca2+-ATPase ACA8, mixing of 0.0006 ml of protein solution, containing 16 mg/ml protein in 25 mM Tris, pH 7.0, 50 mM NaCl, 10 mM 2-mercaptoethanol, 5 mM CaCl2, with 0.001 ml reservoir solution, containing 2.0 M ammonium sulfate, 0.1 M CAPS, pH 10.5, 0.2 M lithium sulfate, at final pH 8.2, ar 20°C, X-ray diffraction structure determination and analysis at 3.0 A resolution
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
R123I
site-directed mutagenesis, when Arg123 of ShMTP1 is mutated to Ile, the ability to confer Mn tolerance to either yeast or Arabidopsis is completely lost
A56S
-
the mutation leads to lowered apparent affinity of the PMCA isoform ACA8 for phosphatidylinositol 4-monophosphate by 2-3fold
R59A
-
the mutation leads to lowered apparent affinity of the PMCA isoform ACA8 for phosphatidylinositol 4-monophosphate by 2-3fold
S19D
the mutant with 163% of wild type activity is deregulated by showing low activation by calmodulin and tryptic cleavage of the N-terminus
S22D
the mutant with wild type activity is deregulated by showing low activation by calmodulin and tryptic cleavage of the N-terminus
S27D
the mutant with 89% of wild type activity is deregulated by showing low activation by calmodulin and tryptic cleavage of the N-terminus
S57D
the mutant with 120% of wild type activity is deregulated by showing low activation by calmodulin and tryptic cleavage of the N-terminus. The mutant shows 10fold higher affinity towards calmodulin compared to the wild type enzyme
S99D
the mutant with 77% of wild type activity shows half of the wild type affinity towards calmodulin
Y62A
-
the mutation leads to lowered apparent affinity of the PMCA isoform ACA8 for phosphatidylinositol 4-monophosphate by 2-3fold
additional information
additional information
recombinant ECA1 shows ability to confer tolerance to toxic concentrations of Mn when heterologously expressed in a Mn-sensitive mutant yeast strain. The Arabidopsis IAA-leucine resistant 2 (ilr2) mutant has a slight tolerance to Mn stress. Transport characterization of microsomal membrane vesicles from ilr2 plants demonstrates a significant increase in ATP-dependent Mn2+ transport compared to wild-type plants
additional information
-
the N-deleted mutant DELTA74-ACA8 is also activated by acidic phospholipids
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
nickel-NTA-agarose column chromatography and glutathione-Sepharose column chromatography
recombinant His6-tagged ACA8 residues 40-95, comprising the calmodulin binding site of the enzyme, from Escherichia coli by nickel affinity chromatography and gel filtration to homogeneity
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
ECA3 mutant defective in its endogenous Ca21 pumps is expressed in Saccharomyces cerevisiae strain K616
ECA3 mutant defective in its endogenous Ca21 pumps is expressed in Saccharomyces cerevisiae strain K616
expressed in Saccharomyces cerevisiae mutant strain K616 devoid of endogenous Ca2+-ATPases
expressed in Saccharomyces cerevisiae strain K616
expression of ACA8 residues 40-95, comprising the calmodulin binding site of the enzyme, in Escherichia coli as protein with an N-terminal fusion consisting of a His6 tag, a lipoyl domain and a TEV protease cleavage site
-
mutant enzymes are expressed in Saccharomyces cerevisiae strain K616 (devoid of endogenous Ca2+-ATPases) and His-tagged N-termini of wild type and mutant proteins are expressed in Escherichia coli strain DH5alpha
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
the ability to manipulate metal transporters, such as by altering substrate specificity, is an essential step in developing genetically engineered plants that can be used for phytoremediation strategies for specific metals
biotechnology
the ability to manipulate metal transporters, such as by altering substrate specificity, is an essential step in developing genetically engineered plants that can be used for phytoremediation strategies for specific metals
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Meneghelli, S.; Fusca, T.; Luoni, L.; De Michelis, M.I.
Dual mechanism of activation of plant plasma membrane Ca2+-ATPase by acidic phospholipids: evidence for a phospholipid binding site which overlaps the calmodulin-binding site
Mol. Membr. Biol.
25
539-546
2008
Arabidopsis thaliana
Li, X.; Chanroj, S.; Wu, Z.; Romanowsky, S.M.; Harper, J.F.; Sze, H.
A distinct endosomal Ca2+/Mn2+ pump affects root growth through the secretory process
Plant Physiol.
147
1675-1689
2008
Arabidopsis thaliana (O23087), Arabidopsis thaliana (P92939), Arabidopsis thaliana (Q9SY55), Arabidopsis thaliana (Q9XES1)
Tidow, H.; Hein, K.L.; Baekgaard, L.; Palmgren, M.G.; Nissen, P.
Expression, purification, crystallization and preliminary X-ray analysis of calmodulin in complex with the regulatory domain of the plasma-membrane Ca2+-ATPase ACA8
Acta Crystallogr. Sect. F
66
361-363
2010
Arabidopsis thaliana
Bonza, M.C.; Luoni, L.
Plant and animal type 2B Ca2+-ATPases: evidence for a common auto-inhibitory mechanism
FEBS Lett.
584
4783-4788
2010
Arabidopsis thaliana (Q9LF79)
Giacometti, S.; Marrano, C.A.; Bonza, M.C.; Luoni, L.; Limonta, M.; De Michelis, M.I.
Phosphorylation of serine residues in the N-terminus modulates the activity of ACA8, a plasma membrane Ca2+-ATPase of Arabidopsis thaliana
J. Exp. Bot.
63
1215-1224
2012
Arabidopsis thaliana (Q9LF79), Arabidopsis thaliana
Bonza, M.C.; De Michelis, M.I.
The plant Ca2+-ATPase repertoire: biochemical features and physiological functions
Plant Biol.
13
421-430
2011
Arabidopsis thaliana
Galva, C.; Virgin, G.K.; Helms, J.B.; Gatto, C.
ATP protects against FITC labeling of Solanum lycopersicon and Arabidopsis thaliana Ca2+-ATPase ATP binding domains
Plant Physiol. Biochem.
71
261-267
2013
Arabidopsis thaliana, Solanum lycopersicum
Astegno, A.; Bonza, M.C.; Vallone, R.; La Verde, V.; D'Onofrio, M.; Luoni, L.; Molesini, B.; Dominici, P.
Arabidopsis calmodulin-like protein CML36 is a calcium (Ca2+) sensor that interacts with the plasma membrane Ca2+-ATPase isoform ACA8 and stimulates its activity
J. Biol. Chem.
292
15049-15061
2017
Arabidopsis thaliana (Q9LF79)
EXTERNAL LINKS (specific for EC-Number 7.2.2.10)
Transporter Classification Database (TCDB): 3.A.3.2.10, 3.A.3.2.14, 3.A.3.2.17, 3.A.3.2.34, 3.A.3.2.3, 3.A.3.2.1, 3.A.3.2.5, 3.A.3.2.9, 3.A.3.2.35, 3.A.3.2.2, 3.A.3.9.2, 3.A.3.2.19, 3.A.3.2.25, 3.A.3.2.40, 3.A.3.2.31, 3.A.3.2.42, 3.A.3.2.11, 3.A.3.2.12, 3.A.3.2.43, 3.A.3.2.7, 3.A.3.2.13, 3.A.3.2.27, 3.A.3.2.6, 3.A.3.2.26, 3.A.3.2.21, 3.A.3.2.44, 3.A.3.2.33, 3.A.3.2.30, 3.A.3.2.32
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
