Any feedback?
Information on EC 4.2.1.3 - aconitate hydratase and Organism(s) Bacillus subtilis and UniProt Accession P09339
for references in articles please use BRENDA:EC4.2.1.3Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
4.2.1.3 aconitate hydrataseIUBMB Comments
Besides interconverting citrate and cis-aconitate, it also interconverts cis-aconitate with isocitrate and, hence, interconverts citrate and isocitrate. The equilibrium mixture is 91% citrate, 6% isocitrate and 3% aconitate. cis-Aconitate is used to designate the isomer (Z)-prop-1-ene-1,2,3-tricarboxylate. An iron-sulfur protein, containing a [4Fe-4S] cluster to which the substrate binds.
Specify your search results
Word Map
- 4.2.1.3
-
iron-sulfur
- transferrin
-
tricarboxylic
- dismutase
- fe-s
- succinate
- tca
- malate
-
citric
- cardiac
-
rna-binding
- neurodegenerative
- frataxin
-
krebs
- fumarase
- friedreich
- heme
- ataxia
- parkinson
- overload
-
iron-dependent
- alpha-ketoglutarate
-
stem-loops
- fluorocitrate
-
bioenergetics
-
ferroportin
-
county
- hepcidin
- peroxynitrite
- mnsod
- fluoroacetate
-
georgia
-
cluster-containing
-
iron-deficient
- iscu
-
iron-replete
-
iron-induced
-
iron-mediated
- alabama
-
kennedy
-
itaconic
-
ferrochelatase
- cubane
-
desulfurase
-
nadp-isocitrate
-
rna-protein
-
iron-related
-
soxrs
- l-ferritin
- isopropylmalate
- medicine
- environmental protection
- synthesis
- biotechnology
The taxonomic range for the selected organisms is: Bacillus subtilis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
aconitase, iron regulatory protein, irp-1, ire-bp, macon, iron regulatory protein 1, aconitate hydratase, cytoplasmic aconitase, aconitase a, c-aconitase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
aconitase
Aconitate hydratase
-
-
-
-
cis-aconitase
-
-
-
-
citrate hydro-lyase
-
-
-
-
Ferritin repressor protein
-
-
-
-
hydratase, aconitate
-
-
-
-
IP210
-
-
-
-
IRE-BP
-
-
-
-
Iron regulatory protein
-
-
-
-
iron-responsive element binding protein
-
-
-
-
IRP
-
-
-
-
IRP1
-
-
-
-
Major iron-containing protein
-
-
-
-
MICP
-
-
-
-
aconitase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
elimination
-
-
-
-
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
citrate(isocitrate) hydro-lyase (cis-aconitate-forming)
Besides interconverting citrate and cis-aconitate, it also interconverts cis-aconitate with isocitrate and, hence, interconverts citrate and isocitrate. The equilibrium mixture is 91% citrate, 6% isocitrate and 3% aconitate. cis-Aconitate is used to designate the isomer (Z)-prop-1-ene-1,2,3-tricarboxylate. An iron-sulfur protein, containing a [4Fe-4S] cluster to which the substrate binds.
CAS REGISTRY NUMBER
COMMENTARY
9024-25-3
-
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
(Z)-2-methylaconitate
2-methylisocitrate
the enzyme is involved in the methylcitric acid cycle
-
-
?
additional information
?
-
-
bifunctional protein, showing aconitase activity in presence of iron and RNA binding activity when cells are iron-deprived
-
?
additional information
?
-
-
amino acid residues Arg741 and Gln745 play great role in the aconitase function
-
-
?
additional information
?
-
-
aconitase binds bound to the citrate synthase 5' leader RNA in vitro
-
-
?
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
(Z)-2-methylaconitate
2-methylisocitrate
the enzyme is involved in the methylcitric acid cycle
-
-
?
additional information
?
-
-
bifunctional protein, showing aconitase activity in presence of iron and RNA binding activity when cells are iron-deprived
-
?
additional information
?
-
-
aconitase binds bound to the citrate synthase 5' leader RNA in vitro
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
-
aconitase is a bifunctional enzyme, which can not only interconvert citrate and isocitrate, but also has the RNA binding function similar to the eukaryotic protein IRP-1, iron regulatory protein 1
physiological function
-
aconitase directly regulates citrate synthase production by interacting with the citZ transcript
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
enzyme binds to the 3 untranslated region of transcriptional activator GerE mRNA in in vitro gel shift assays
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C450S
-
mutant is enzymatically inactive, glutamate auxotroph and accumulates citrate. Mutant strain exhibits overexpression of the citB promoter and accumulates high levels of aconitase protein. Mutant strain exhibits increased levels of citrate synthase protein. Mutant enzyme does not bind to the citrate synthase 5' leader RNA in vitro
C517A
-
enzymatically inactive mutant enzyme that still binds iron responsive elements
R740E/Q744E/F661L/I809T/V852A
-
sixfold increase in specific activity compared to wild-type. Mutant strain is defective in sporulation, affecting the expression of deltaK-dependent genes. Accumulation of transcriptional activator GerE mRNa and protein is delayed in the mutant
R741E
-
mutant is designed to be defective in RNA binding. Mutant strain is glutamate prototroph and accumulates citrate. Mutant strain exhibits overexpression of the citB promoter and accumulates high levels of aconitase protein. Mutant strain exhibits increased levels of citrate synthase protein. Mutant enzyme does not bind to the citrate synthase 5' leader RNA in vitro
R741E/Q745E
-
site-directed mutagenesis, the mutant strain exhibits an increased enzymatic activity of aconitase comparing to that of the wild-type strain, because the aconitase protein expression level is significantly increased in the mutant strain
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of wild-type and mutant enzymes in Escherichia coli strain DH5alpha, and in Bacillus subtilis strains GWH1025 and GWH1026, respectively
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Pickworth Glusker, J.
Aconitase
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
5
413-439
1971
Aspergillus niger, Bacillus subtilis, Bos taurus, Saccharomyces cerevisiae, Oryctolagus cuniculus, Glycine max, Rattus norvegicus, Rheum sp., Salmonella enterica subsp. enterica serovar Typhimurium, Sinapis alba, Solanum tuberosum, Sus scrofa
-
Dingman, D.W.; Sonenshein, A.L.
Purification of aconitase from Bacillus subtilis and correlation of its N-terminal amino acid sequence with the sequence of the citB gene
J. Bacteriol.
169
3062-3067
1987
Bacillus subtilis
Alen, C.; Sonenshein, A.L.
Bacillus subtilis aconitase is an RNA-binding protein
Proc. Natl. Acad. Sci. USA
96
10412-10417
1999
Bacillus subtilis
Serio, A.W.; Pechter, K.B.; Sonenshein, A.L.
Bacillus subtilis aconitase is required for efficient late-sporulation gene expression
J. Bacteriol.
188
6396-6405
2006
Bacillus subtilis
Gao, W.; Dai, S.; Liu, Q.; Xu, H.; Bai, Y.; Qiao, M.
Effect of site-directed mutagenesis of citB on the expression and activity of Bacillus subtilis aconitase
Mikrobiologiia
79
774-778
2011
Bacillus subtilis, Bacillus subtilis NK1010
Pechter, K.B.; Meyer, F.M.; Serio, A.W.; Stuelke, J.; Sonenshein, A.L.
Two roles for aconitase in the regulation of tricarboxylic acid branch gene expression in Bacillus subtilis
J. Bacteriol.
195
1525-1537
2013
Bacillus subtilis
Reddick, J.J.; Sirkisoon, S.; Dahal, R.A.; Hardesty, G.; Hage, N.E.; Booth, W.T.; Quattlebaum, A.L.; Mills, S.N.; Meadows, V.G.; Adams, S.L.H.; Doyle, J.S.; Kiel, B.E.
First biochemical characterization of a methylcitric acid cycle from Bacillus subtilis strain 168
Biochemistry
56
5698-5711
2017
Bacillus subtilis (P09339), Bacillus subtilis 168 (P09339)
EXTERNAL LINKS (specific for EC-Number 4.2.1.3)
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
