LSRF_ECOLI
ID LSRF_ECOLI Reviewed; 291 AA.
AC P76143; Q2MB99;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=3-hydroxy-5-phosphonooxypentane-2,4-dione thiolase {ECO:0000255|HAMAP-Rule:MF_02052};
DE EC=2.3.1.245 {ECO:0000255|HAMAP-Rule:MF_02052, ECO:0000269|PubMed:25225400};
GN Name=lsrF {ECO:0000255|HAMAP-Rule:MF_02052}; Synonyms=yneB;
GN OrderedLocusNames=b1517, JW1510;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [3]
RP INDUCTION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15601708; DOI=10.1128/jb.187.1.238-248.2005;
RA Xavier K.B., Bassler B.L.;
RT "Regulation of uptake and processing of the quorum-sensing autoinducer AI-2
RT in Escherichia coli.";
RL J. Bacteriol. 187:238-248(2005).
RN [4]
RP INDUCTION.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=15743955; DOI=10.1128/jb.187.6.2066-2076.2005;
RA Wang L., Hashimoto Y., Tsao C.-Y., Valdes J.J., Bentley W.E.;
RT "Cyclic AMP (cAMP) and cAMP receptor protein influence both synthesis and
RT uptake of extracellular autoinducer 2 in Escherichia coli.";
RL J. Bacteriol. 187:2066-2076(2005).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF APOENZYME AND IN COMPLEXES WITH
RP D-RIBITOL 5-PHOSPHATE AND D-RIBULOSE 5-PHOSPHATE, AND SUBUNIT.
RX PubMed=19714241; DOI=10.1371/journal.pone.0006820;
RA Diaz Z., Xavier K.B., Miller S.T.;
RT "The crystal structure of the Escherichia coli autoinducer-2 processing
RT protein LsrF.";
RL PLoS ONE 4:E6820-E6820(2009).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.51 ANGSTROMS) OF MUTANT ALA-203 IN COMPLEX WITH
RP 3-HYDROXY-5-PHOSPHONOOXYPENTANE-2,4-DIONE, FUNCTION, CATALYTIC ACTIVITY,
RP MUTAGENESIS OF ASP-57; LYS-203 AND ASP-251, BIOPHYSICOCHEMICAL PROPERTIES,
RP AND ACTIVE SITE.
RX PubMed=25225400; DOI=10.1073/pnas.1408691111;
RA Marques J.C., Oh I.K., Ly D.C., Lamosa P., Ventura M.R., Miller S.T.,
RA Xavier K.B.;
RT "LsrF, a coenzyme A-dependent thiolase, catalyzes the terminal step in
RT processing the quorum sensing signal autoinducer-2.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:14235-14240(2014).
CC -!- FUNCTION: Involved in the degradation of phospho-AI-2, thereby
CC terminating induction of the lsr operon and closing the AI-2 signaling
CC cycle. Catalyzes the transfer of an acetyl moiety from 3-hydroxy-5-
CC phosphonooxypentane-2,4-dione to CoA to form glycerone phosphate and
CC acetyl-CoA. {ECO:0000255|HAMAP-Rule:MF_02052,
CC ECO:0000269|PubMed:25225400}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + dihydroxyacetone phosphate = 3-hydroxy-2,4-
CC dioxopentyl phosphate + CoA; Xref=Rhea:RHEA:44736, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:57642, ChEBI:CHEBI:84359;
CC EC=2.3.1.245; Evidence={ECO:0000255|HAMAP-Rule:MF_02052,
CC ECO:0000269|PubMed:25225400};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Note=kcat is 127 sec(-1). {ECO:0000269|PubMed:25225400};
CC -!- SUBUNIT: Homodecamer. {ECO:0000255|HAMAP-Rule:MF_02052,
CC ECO:0000269|PubMed:19714241}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02052}.
CC -!- INDUCTION: In the absence of AI-2, repressed by LsrR. Induced by AI-2,
CC via release of the LsrR repressor. In the absence of glucose, induced
CC by cAMP-CRP by direct binding to the upstream region of the lsr
CC promoter. {ECO:0000269|PubMed:15601708, ECO:0000269|PubMed:15743955}.
CC -!- SIMILARITY: Belongs to the DeoC/FbaB aldolase family.
CC {ECO:0000255|HAMAP-Rule:MF_02052, ECO:0000305}.
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DR EMBL; U00096; AAC74590.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76457.1; -; Genomic_DNA.
DR PIR; H64905; H64905.
DR RefSeq; NP_416034.1; NC_000913.3.
DR RefSeq; WP_000774165.1; NZ_SSZK01000001.1.
DR PDB; 3GKF; X-ray; 2.90 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T=1-291.
DR PDB; 3GLC; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T=1-291.
DR PDB; 3GND; X-ray; 2.90 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T=1-291.
DR PDB; 4P2V; X-ray; 2.51 A; A/B/C/D/E/F/G/H/I/K=1-291.
DR PDBsum; 3GKF; -.
DR PDBsum; 3GLC; -.
DR PDBsum; 3GND; -.
DR PDBsum; 4P2V; -.
DR AlphaFoldDB; P76143; -.
DR SMR; P76143; -.
DR BioGRID; 4261350; 18.
DR BioGRID; 850431; 1.
DR DIP; DIP-12754N; -.
DR IntAct; P76143; 5.
DR STRING; 511145.b1517; -.
DR jPOST; P76143; -.
DR PaxDb; P76143; -.
DR PRIDE; P76143; -.
DR EnsemblBacteria; AAC74590; AAC74590; b1517.
DR EnsemblBacteria; BAE76457; BAE76457; BAE76457.
DR GeneID; 946071; -.
DR KEGG; ecj:JW1510; -.
DR KEGG; eco:b1517; -.
DR PATRIC; fig|1411691.4.peg.750; -.
DR EchoBASE; EB3571; -.
DR eggNOG; COG1830; Bacteria.
DR HOGENOM; CLU_057069_1_0_6; -.
DR InParanoid; P76143; -.
DR OMA; CEYWGMP; -.
DR PhylomeDB; P76143; -.
DR BioCyc; EcoCyc:G6804-MON; -.
DR BioCyc; MetaCyc:G6804-MON; -.
DR BRENDA; 2.3.1.245; 2026.
DR EvolutionaryTrace; P76143; -.
DR PRO; PR:P76143; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IDA:EcoCyc.
DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:InterPro.
DR CDD; cd00958; DhnA; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_02052; LsrF; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR002915; DeoC/FbaB/LacD_aldolase.
DR InterPro; IPR041720; FbaB-like.
DR InterPro; IPR033673; LsrF.
DR Pfam; PF01791; DeoC; 1.
DR PIRSF; PIRSF038992; Aldolase_Ia; 1.
DR SMART; SM01133; DeoC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Reference proteome; Schiff base; Transferase.
FT CHAIN 1..291
FT /note="3-hydroxy-5-phosphonooxypentane-2,4-dione thiolase"
FT /id="PRO_0000138945"
FT ACT_SITE 203
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02052,
FT ECO:0000269|PubMed:25225400"
FT MUTAGEN 57
FT /note="D->A: No activity."
FT /evidence="ECO:0000269|PubMed:25225400"
FT MUTAGEN 203
FT /note="K->A: No activity."
FT /evidence="ECO:0000269|PubMed:25225400"
FT MUTAGEN 251
FT /note="D->A: No activity."
FT /evidence="ECO:0000269|PubMed:25225400"
FT HELIX 34..43
FT /evidence="ECO:0007829|PDB:3GLC"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:3GLC"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:3GLC"
FT HELIX 59..62
FT /evidence="ECO:0007829|PDB:3GLC"
FT HELIX 71..74
FT /evidence="ECO:0007829|PDB:3GLC"
FT HELIX 76..81
FT /evidence="ECO:0007829|PDB:3GLC"
FT STRAND 83..87
FT /evidence="ECO:0007829|PDB:3GLC"
FT HELIX 89..95
FT /evidence="ECO:0007829|PDB:3GLC"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:3GLC"
FT STRAND 104..107
FT /evidence="ECO:0007829|PDB:3GLC"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:4P2V"
FT HELIX 127..132
FT /evidence="ECO:0007829|PDB:3GLC"
FT STRAND 136..142
FT /evidence="ECO:0007829|PDB:3GLC"
FT HELIX 149..164
FT /evidence="ECO:0007829|PDB:3GLC"
FT TURN 165..167
FT /evidence="ECO:0007829|PDB:3GLC"
FT STRAND 170..174
FT /evidence="ECO:0007829|PDB:3GLC"
FT HELIX 184..196
FT /evidence="ECO:0007829|PDB:3GLC"
FT STRAND 200..205
FT /evidence="ECO:0007829|PDB:3GLC"
FT TURN 208..210
FT /evidence="ECO:0007829|PDB:3GLC"
FT HELIX 211..216
FT /evidence="ECO:0007829|PDB:3GLC"
FT STRAND 222..225
FT /evidence="ECO:0007829|PDB:3GLC"
FT HELIX 232..244
FT /evidence="ECO:0007829|PDB:3GLC"
FT STRAND 248..253
FT /evidence="ECO:0007829|PDB:3GLC"
FT HELIX 254..257
FT /evidence="ECO:0007829|PDB:3GLC"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:3GLC"
FT HELIX 262..275
FT /evidence="ECO:0007829|PDB:3GLC"
FT HELIX 279..287
FT /evidence="ECO:0007829|PDB:3GLC"
SQ SEQUENCE 291 AA; 31893 MW; D5CC245A5C709F1C CRC64;
MADLDDIKDG KDFRTDQPQK NIPFTLKGCG ALDWGMQSRL SRIFNPKTGK TVMLAFDHGY
FQGPTTGLER IDINIAPLFE HADVLMCTRG ILRSVVPPAT NRPVVLRASG ANSILAELSN
EAVALSMDDA VRLNSCAVAA QVYIGSEYEH QSIKNIIQLV DAGMKVGMPT MAVTGVGKDM
VRDQRYFSLA TRIAAEMGAQ IIKTYYVEKG FERIVAGCPV PIVIAGGKKL PEREALEMCW
QAIDQGASGV DMGRNIFQSD HPVAMMKAVQ AVVHHNETAD RAYELYLSEK Q
