ID   LSRF_SALCH              Reviewed;         291 AA.
AC   Q57HD9;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 84.
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=SCH_3967;
OS   Salmonella choleraesuis (strain SC-B67).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=321314;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC-B67;
RX   PubMed=15781495; DOI=10.1093/nar/gki297;
RA   Chiu C.-H., Tang P., Chu C., Hu S., Bao Q., Yu J., Chou Y.-Y., Wang H.-S.,
RA   Lee Y.-S.;
RT   "The genome sequence of Salmonella enterica serovar Choleraesuis, a highly
RT   invasive and resistant zoonotic pathogen.";
RL   Nucleic Acids Res. 33:1690-1698(2005).
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; AE017220; AAX67873.1; -; Genomic_DNA.
DR   RefSeq; WP_000774147.1; NC_006905.1.
DR   AlphaFoldDB; Q57HD9; -.
DR   SMR; Q57HD9; -.
DR   EnsemblBacteria; AAX67873; AAX67873; SCH_3967.
DR   KEGG; sec:SCH_3967; -.
DR   HOGENOM; CLU_057069_1_0_6; -.
DR   OMA; CEYWGMP; -.
DR   Proteomes; UP000000538; 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_0000351526"
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