ID   LSRF_SALPB              Reviewed;         291 AA.
AC   A9MZG5;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 83.
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=SPAB_05052;
OS   Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=1016998;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1250 / SPB7;
RG   The Salmonella enterica serovar Paratyphi B Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Fulton R., Cordes M., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the DeoC/FbaB aldolase family.
CC       {ECO:0000255|HAMAP-Rule:MF_02052}.
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DR   EMBL; CP000886; ABX70343.1; -; Genomic_DNA.
DR   RefSeq; WP_000774144.1; NC_010102.1.
DR   AlphaFoldDB; A9MZG5; -.
DR   SMR; A9MZG5; -.
DR   KEGG; spq:SPAB_05052; -.
DR   PATRIC; fig|1016998.12.peg.4742; -.
DR   HOGENOM; CLU_057069_1_0_6; -.
DR   OMA; CEYWGMP; -.
DR   BioCyc; SENT1016998:SPAB_RS20560-MON; -.
DR   Proteomes; UP000008556; 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   3: Inferred from homology;
KW   Cytoplasm; Schiff base; Transferase.
FT   CHAIN           1..291
FT                   /note="3-hydroxy-5-phosphonooxypentane-2,4-dione thiolase"
FT                   /id="PRO_0000351528"
FT   ACT_SITE        203
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02052"
SQ   SEQUENCE   291 AA;  31729 MW;  1343B5149CDE9EC5 CRC64;
     MADLDDIKDG KDFHTDKPQT NTLFALKGCG ALDWGMQSRL ARIFNPKTRK TVMLAFDHGY
     FQGPTTGLER IDINIAPLFE YADVLMCTRG ILRSVVPPAI NKPVVLRASG ANSILTELSN
     EAVAVAMDDA VRLNSCAAAA QVYIGSEHEH QSIKNIIQLI DAGLRVGMPI MAVTGVGKDM
     ARDQRYFSLA TRIAAEMGAQ IIKTYYVDKG FERIAAGCPV PIVIAGGKKL LEREALEMCY
     QAIDQGASGV DMGRNIFQSE DPVAMIKAVH AVVHHNETAE RAYELFLSEK G