LSRF_SALTY
ID LSRF_SALTY Reviewed; 291 AA.
AC Q8ZKQ0;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 103.
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};
GN Name=lsrF {ECO:0000255|HAMAP-Rule:MF_02052}; OrderedLocusNames=STM4078;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP INDUCTION.
RC STRAIN=ATCC 14028 / SGSG 2980 / CDC 6516-60 / NCTC 12023;
RX PubMed=11722742; DOI=10.1046/j.1365-2958.2001.02669.x;
RA Taga M.E., Semmelhack J.L., Bassler B.L.;
RT "The LuxS-dependent autoinducer AI-2 controls the expression of an ABC
RT transporter that functions in AI-2 uptake in Salmonella typhimurium.";
RL Mol. Microbiol. 42:777-793(2001).
RN [3]
RP PRELIMINARY FUNCTION, AND INDUCTION.
RC STRAIN=ATCC 14028 / SGSG 2980 / CDC 6516-60 / NCTC 12023;
RX PubMed=14622426; DOI=10.1046/j.1365-2958.2003.03781.x;
RA Taga M.E., Miller S.T., Bassler B.L.;
RT "Lsr-mediated transport and processing of AI-2 in Salmonella typhimurium.";
RL Mol. Microbiol. 50:1411-1427(2003).
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 -!- 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 -!- SUBUNIT: Homodecamer. {ECO:0000255|HAMAP-Rule:MF_02052}.
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. {ECO:0000269|PubMed:11722742,
CC ECO:0000269|PubMed:14622426}.
CC -!- SIMILARITY: Belongs to the DeoC/FbaB aldolase family.
CC {ECO:0000255|HAMAP-Rule:MF_02052}.
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DR EMBL; AE006468; AAL22918.1; -; Genomic_DNA.
DR RefSeq; NP_462959.1; NC_003197.2.
DR RefSeq; WP_000774147.1; NC_003197.2.
DR AlphaFoldDB; Q8ZKQ0; -.
DR SMR; Q8ZKQ0; -.
DR STRING; 99287.STM4078; -.
DR PaxDb; Q8ZKQ0; -.
DR EnsemblBacteria; AAL22918; AAL22918; STM4078.
DR GeneID; 1255605; -.
DR KEGG; stm:STM4078; -.
DR PATRIC; fig|99287.12.peg.4298; -.
DR HOGENOM; CLU_057069_1_0_6; -.
DR OMA; CEYWGMP; -.
DR PhylomeDB; Q8ZKQ0; -.
DR BioCyc; SENT99287:STM4078-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:UniProtKB-UniRule.
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 2: Evidence at transcript level;
KW Cytoplasm; Reference proteome; Schiff base; Transferase.
FT CHAIN 1..291
FT /note="3-hydroxy-5-phosphonooxypentane-2,4-dione thiolase"
FT /id="PRO_0000351530"
FT ACT_SITE 203
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02052"
SQ SEQUENCE 291 AA; 31743 MW; 1EC3B51480C29ED9 CRC64;
MADLDDIKDG KDFHTDKPQT NTLFALKGCG ALDWGMQSRL ARIFNPKTRK TVMLAFDHGY
FQGPTTGLER IDINIAPLFE YADVLMCTRG ILRSVVPPAI NKPVVLRASG ANSILTELSN
EAVAVAMDDA VRLNSCAAAA QVYIGSEHEH QSIKNIIQLI DAGLRVGMPI MAVTGVGKDM
ARDQRYFSLA TRIAAEMGAQ IIKTYYVDKG FERIAAGCPV PIVIAGGKKL PEREALEMCY
QAIDQGASGV DMGRNIFQSE DPVAMIKAVH AVVHHNETAE RAYELFLSEK S
