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Information on EC 2.3.1.245 - 3-hydroxy-5-phosphooxypentane-2,4-dione thiolase and Organism(s) Escherichia coli

for references in articles please use BRENDA:EC2.3.1.245
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IUBMB Comments
The enzyme participates in a degradation pathway of the bacterial quorum-sensing autoinducer molecule AI-2.
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This record set is specific for:
Escherichia coli
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The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
3-hydroxy-5-phosphonooxypentane-2,4-dione thiolase, lsrF, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3-hydroxy-5-phosphonooxypentane-2,4-dione thiolase
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:glycerone phosphate C-acetyltransferase
The enzyme participates in a degradation pathway of the bacterial quorum-sensing autoinducer molecule AI-2.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-hydroxy-5-phosphonooxypentane-2,4-dione + coenzyme A
glycerone phosphate + acetyl-CoA
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
3-hydroxy-5-phosphonooxypentane-2,4-dione + coenzyme A
glycerone phosphate + acetyl-CoA
show the reaction diagram
the enzyme participates in a degradation pathway of the bacterial quorum-sensing autoinducer molecule AI-2 i.e. (S)-4,5-dihydroxypentane-2,3-dione
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
the enzyme participates in a degradation pathway of the bacterial quorum-sensing autoinducer molecule AI-2
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
A0A154CH76_ECOLX
291
0
31802
TrEMBL
-
A0A152XLG3_ECOLX
291
0
31837
TrEMBL
-
A0A400LH36_ECOLX
291
0
31803
TrEMBL
-
A0A229AX43_ECOLX
291
0
31814
TrEMBL
-
A0A6S4WIV7_ECOLX
291
0
31907
TrEMBL
-
A0A827URC1_ECOLX
291
0
31911
TrEMBL
-
A0A7D7DHQ8_ECOLX
291
0
31851
TrEMBL
-
A0A1V3VWX8_ECOLX
291
0
31821
TrEMBL
-
A0A1M0SMY3_ECOLX
291
0
31823
TrEMBL
-
A0A8H1EE87_ECOLX
291
0
31907
TrEMBL
-
A0A826X8J0_ECOLX
291
0
31835
TrEMBL
-
A0A2S8I4H4_ECOLX
291
0
31772
TrEMBL
-
A0A828HBA6_ECOLX
291
0
31851
TrEMBL
-
A0A0A1A500_ECOLX
291
0
31864
TrEMBL
-
A0A827YE45_ECOLX
291
0
31892
TrEMBL
-
A0A037Y2J9_ECOLX
291
0
31851
TrEMBL
-
A0A0V9GEZ5_ECOLX
291
0
31851
TrEMBL
-
A0A827CS64_ECOLX
291
0
31893
TrEMBL
-
A0A6D0EI88_ECOLX
264
0
28365
TrEMBL
-
A0A6N4P3X8_ECOLX
291
0
31809
TrEMBL
-
A0A6D0UX73_ECOLX
291
0
31901
TrEMBL
-
A0A090J8M0_ECOLX
291
0
31893
TrEMBL
-
A0A8H0EEW8_ECOLX
291
0
31895
TrEMBL
-
A0A3Q0MXX6_ECOLX
291
0
31878
TrEMBL
-
C3T9W8_ECOLX
291
0
31895
TrEMBL
-
A0A7L7E902_ECOLX
291
0
31884
TrEMBL
-
A0A1Y2XVK5_ECOLX
291
0
31855
TrEMBL
-
A0A827BJ73_ECOLX
291
0
31877
TrEMBL
-
A0A8H9T8I2_ECOLX
286
0
31307
TrEMBL
-
A0A3T4J6K7_ECOLX
291
0
31879
TrEMBL
-
A0A1M0D094_ECOLX
291
0
31837
TrEMBL
-
A0A828M1M5_ECOLX
291
0
31879
TrEMBL
-
A0A0F3WN47_ECOLX
289
0
31396
TrEMBL
-
A0A136WTJ9_ECOLX
291
0
31867
TrEMBL
-
A0A8G8BNR9_ECOLX
291
0
31882
TrEMBL
-
A0A8B5KIG8_ECOLX
291
0
31893
TrEMBL
-
A0A3S6ZF87_ECOLX
291
0
31895
TrEMBL
-
A0A6G4C288_ECOLX
291
0
31877
TrEMBL
-
A0A244B9V6_ECOLX
291
0
31775
TrEMBL
-
A0A447XXH5_ECOLX
291
0
31884
TrEMBL
-
A0A769DD91_ECOLX
291
0
31885
TrEMBL
-
A0A4Y7Z8F5_ECOLX
298
0
32393
TrEMBL
-
A0A7L5V4I0_ECOLX
291
0
31876
TrEMBL
-
A0A377LF31_ECOLX
291
0
31851
TrEMBL
-
A0A0L7ADH3_ECOLX
291
0
31850
TrEMBL
-
A0A377CKK4_ECOLX
291
0
31877
TrEMBL
-
A0A3L9HV24_ECOLX
281
0
30625
TrEMBL
-
A0A246NP67_ECOLX
291
0
31893
TrEMBL
-
A0A3U6G8S0_ECOLX
291
0
31850
TrEMBL
-
A0A6C9JRC4_ECOLX
291
0
31821
TrEMBL
-
C3T9W7_ECOLX
291
0
31865
TrEMBL
-
A0A831CL43_ECOLX
291
0
31863
TrEMBL
-
A0A8H9XL45_ECOLX
291
0
31847
TrEMBL
-
A0A241QRP5_ECOLX
291
0
31883
TrEMBL
-
A0A0F3U6H5_ECOLX
291
0
31923
TrEMBL
-
A0A193LSS4_ECOLX
291
0
31865
TrEMBL
-
A0A066RHZ6_ECOLX
291
0
31877
TrEMBL
-
A0A6C8TX48_ECOLX
291
0
31849
TrEMBL
-
J7Q7I1_ECOLX
291
0
31865
TrEMBL
-
A0A8I0NRF1_ECOLX
291
0
31839
TrEMBL
-
A0A822UE53_ECOLX
291
0
31865
TrEMBL
-
A0A0D8WF39_ECOLX
291
0
31837
TrEMBL
-
A0A0J2EMQ2_ECOLX
291
0
31805
TrEMBL
-
A0A3L2NMU2_ECOLX
291
0
31872
TrEMBL
-
A0A244BTP9_ECOLX
291
0
31865
TrEMBL
-
A0A8G9AV60_ECOLX
291
0
31907
TrEMBL
-
A0A827IRZ0_ECOLX
291
0
31895
TrEMBL
-
A0A8H1SWF8_ECOLX
291
0
31807
TrEMBL
-
A0A6D1B1Y3_ECOLX
291
0
31909
TrEMBL
-
A0A6M1IUC8_ECOLX
291
0
31879
TrEMBL
-
A0A2X1JVQ1_ECOLX
291
0
31881
TrEMBL
-
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decamer
each monomer having an (alphabeta)8-barrel fold, crystalligraphic data
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals of the catalytically inactive mutant enzyme K203A
hanging drop method with a well solution of 22% PEG 400, 200 mM MgCl2, 100 mM Tris pH 8.0
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K203A
inactive mutant enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli strain BL21
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Diaz, Z.; Xavier, K.B.; Miller, S.T.
The crystal structure of the Escherichia coli autoinducer-2 processing protein LsrF
PLoS One
4
e6820
2009
Escherichia coli (P76143)
Manually annotated by BRENDA team
Marques, J.C.; Oh, I.K.; Ly, D.C.; Lamosa, P.; Ventura, M.R.; Miller, S.T.; Xavier, K.B.
LsrF, a coenzyme A-dependent thiolase, catalyzes the terminal step in processing the quorum sensing signal autoinducer-2
Proc. Natl. Acad. Sci. USA
111
14235-14240
2014
Escherichia coli (P76143)
Manually annotated by BRENDA team