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 24-JAN-2024, entry version 142. 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; Pseudomonadota; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 511145-b1517; -. DR EnsemblBacteria; AAC74590; AAC74590; b1517. 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 OrthoDB; 5915071at2; -. DR PhylomeDB; P76143; -. DR BioCyc; EcoCyc:G6804-MONOMER; -. DR BioCyc; MetaCyc:G6804-MONOMER; -. DR BRENDA; 2.3.1.245; 2026. DR EvolutionaryTrace; P76143; -. DR PHI-base; PHI:9996; -. 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; Aldolase class I; 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 PANTHER; PTHR47916:SF1; 3-HYDROXY-5-PHOSPHONOOXYPENTANE-2,4-DIONE THIOLASE-RELATED; 1. DR PANTHER; PTHR47916; FRUCTOSE-BISPHOSPHATE ALDOLASE CLASS 1; 1. DR Pfam; PF01791; DeoC; 1. DR PIRSF; PIRSF038992; Aldolase_Ia; 1. DR SMART; SM01133; DeoC; 1. DR SUPFAM; SSF51569; Aldolase; 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 //