Information on EC 3.6.3.30 - Fe3+-transporting ATPase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
3.6.3.30
-
RECOMMENDED NAME
GeneOntology No.
Fe3+-transporting ATPase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + H2O + Fe3+/out = ADP + phosphate + Fe3+/in
show the reaction diagram
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
-
-
-
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transmembrane transport
SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (ferric-ion-transporting)
ABC-type (ATP-binding cassette-type) ATPase, characterized by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. A bacterial enzyme that imports ferric cations.
CAS REGISTRY NUMBER
COMMENTARY hide
9000-83-3
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain 3937
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-
Manually annotated by BRENDA team
strain 3937
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-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain W225
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-
Manually annotated by BRENDA team
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 + Fe3+/out
ADP + phosphate + Fe3+/in
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + H2O + Fe3+/out
ADP + phosphate + Fe3+/in
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe3+
-
YfuA is able to coordinate a single Fe3+ ion in an octahedral fashion, utilizing five amino acid residues
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
amino-oxyacetic acid
aminoethoxyvinylglycine
gallium
silver thiosulfate
sodium orthovanadate
-
-
additional information
-
not inhibitory: carbonyl cyanide m-chlorophenyl hydrazone
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0009 - 0.0012
Fe3+
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
radio-labeled iron transport assay
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40000
-
x * 40000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heteromer
-
-
consists of FitA, FitB, FitC, FitD, FitE and FitR
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
lipoprotein
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
1.8 A structure of iron-free SfuA
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1.8 A structure of iron-loaded YfuA
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
apo-FbpA is purified by cetyltrimethylammonium bromide extraction and by using a carboxymethyl Sepharose column
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ABC7 gene
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complementing plasmids are constructed, a FhuC K42N mutant is constructed
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expression in Escherichia coli
for expression in Escherichia coli cells
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the FbpA gene from Neisseria gonorrhoeae strain F62 is cloned for expression of the protein in Escherichia coli cells
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E149Q
-
effect of motif 1 and 2 mutations on transport is measured, remaining transport rate 95%
F162L
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effect of motif 1 and 2 mutations on transport is measured, remaining transport rate 104%
G155A
-
effect of motif 1 and 2 mutations on transport is measured, remaining transport rate 76%
G155E
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effect of motif 1 and 2 mutations on transport is measured, remaining transport rate 111%
G155V
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effect of motif 1 and 2 mutations on transport is measured, remaining transport rate 88%
G418A
-
effect of motif 1 and 2 mutations on transport is measured, remaining transport rate 38%
I174F
-
effect of permease mutaion on transport is measured, remaining transport rate 27%
I174N
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effect of permease mutaion on transport is measured, remaining transport rate 89%
I174N/S475I
-
effect of permease mutaion on transport is measured, remaining transport rate 9%
I383N
-
effect of permease mutaion on transport is measured, remaining transport rate 100%
I497V
-
effect of permease mutaion on transport is measured, remaining transport rate 100%
L154D
-
effect of motif 1 and 2 mutations on transport is measured, remaining transport rate 35%
L417D
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effect of motif 1 and 2 mutations on transport is measured, remaining transport rate 5%
P168A
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effect of motif 1 and 2 mutations on transport is measured, remaining transport rate 116%
S146Y
-
effect of permease mutaion on transport is measured, remaining transport rate 18%
S153A
-
effect of motif 1 and 2 mutations on transport is measured, remaining transport rate 112%
S475I
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effect of permease mutaion on transport is measured, remaining transport rate 12%
V497I
-
effect of permease mutaion on transport is measured, remaining transport rate 23%
Y196I
-
mutation in periplasmic biding protein, FbpA, greatly diminishes iron binding affinity, but has about 35% of wild-type transport activity
E164D
-
mutant in nucleotide-binding domain fbpC, 10fold reduction in specific activity
K42N
-
FhuC mutant
additional information
-
a Staphylococcus aureus fhuCBG deletion strain is constructed and characterized
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