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IUBMB CommentsThe enzyme participates in a degradation pathway of the bacterial quorum-sensing autoinducer molecule AI-2.
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
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3-hydroxy-5-phosphonooxypentane-2,4-dione thiolase
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acetyl-CoA:glycerone phosphate C-acetyltransferase
The enzyme participates in a degradation pathway of the bacterial quorum-sensing autoinducer molecule AI-2.
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3-hydroxy-5-phosphonooxypentane-2,4-dione + coenzyme A
glycerone phosphate + acetyl-CoA
3-hydroxy-5-phosphonooxypentane-2,4-dione + coenzyme A
glycerone phosphate + acetyl-CoA
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3-hydroxy-5-phosphonooxypentane-2,4-dione + coenzyme A
glycerone phosphate + acetyl-CoA
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
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3-hydroxy-5-phosphonooxypentane-2,4-dione + coenzyme A
glycerone phosphate + acetyl-CoA
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
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SwissProt
brenda
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metabolism
the enzyme participates in a degradation pathway of the bacterial quorum-sensing autoinducer molecule AI-2
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
A0A154CH76_ECOLX
291
0
31802
TrEMBL
-
A0A152XLG3_ECOLX
291
0
31837
TrEMBL
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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
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decamer
each monomer having an (alphabeta)8-barrel fold, crystalligraphic data
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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
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K203A
inactive mutant enzyme
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expression in Escherichia coli strain BL21
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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)
brenda
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)
brenda