ID   LSRF_SHIF8              Reviewed;         256 AA.
AC   Q0T4L4;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=3-hydroxy-5-phosphonooxypentane-2,4-dione thiolase {ECO:0000250|UniProtKB:P76143};
DE            EC=2.3.1.245 {ECO:0000250|UniProtKB:P76143};
GN   Name=lsrF; OrderedLocusNames=SFV_1574;
OS   Shigella flexneri serotype 5b (strain 8401).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=373384;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=8401;
RX   PubMed=16822325; DOI=10.1186/1471-2164-7-173;
RA   Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z., Peng J.,
RA   Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y., Jin Q.;
RT   "Complete genome sequence of Shigella flexneri 5b and comparison with
RT   Shigella flexneri 2a.";
RL   BMC Genomics 7:173-173(2006).
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:0000250|UniProtKB:P76143}.
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:0000250|UniProtKB:P76143};
CC   -!- SUBUNIT: Homodecamer. {ECO:0000250|UniProtKB:P76143}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the DeoC/FbaB aldolase family. {ECO:0000305}.
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DR   EMBL; CP000266; ABF03751.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q0T4L4; -.
DR   SMR; Q0T4L4; -.
DR   EnsemblBacteria; ABF03751; ABF03751; SFV_1574.
DR   KEGG; sfv:SFV_1574; -.
DR   HOGENOM; CLU_057069_1_0_6; -.
DR   OMA; CEYWGMP; -.
DR   BioCyc; SFLE373384:SFV_RS08820-MON; -.
DR   Proteomes; UP000000659; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   CDD; cd00958; DhnA; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR002915; DeoC/FbaB/LacD_aldolase.
DR   InterPro; IPR041720; FbaB-like.
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..256
FT                   /note="3-hydroxy-5-phosphonooxypentane-2,4-dione thiolase"
FT                   /id="PRO_0000351532"
FT   ACT_SITE        168
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P76143"
SQ   SEQUENCE   256 AA;  27990 MW;  EE6DC805158EDE31 CRC64;
     MQSRLSWIFN PKTGKTVMLA FDHGYFQGPT TGLERIDINI APLFEHADVL MCTRGILRSV
     VPPATNKPGV LRASGANSIL AELSNEAVAL SMDDAVRLNS CAVAAQVYIG SEYEHQSIKN
     IIQLVDAGMK VGMPTMAVTG VGKDMVRDQR YFSLATRIAA EMGAQIIKTY YVEKGFERIV
     AGCPVPIVIA GGKKLPERET LEMCWQAIDQ GASGVDMGRN IFQSDHPVAM MKAVQAVVHH
     NETADRAYEL YLSEKQ