ID   LSRF_SHIFL              Reviewed;         256 AA.
AC   Q83L15; Q7UCG5;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 109.
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=SF1578, S1704;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA   Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA   Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA   Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA   Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA   Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella flexneri
RT   serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(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: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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAP17058.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE005674; AAN43166.1; -; Genomic_DNA.
DR   EMBL; AE014073; AAP17058.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_707459.1; NC_004337.2.
DR   RefSeq; WP_001191842.1; NZ_WPGW01000239.1.
DR   AlphaFoldDB; Q83L15; -.
DR   SMR; Q83L15; -.
DR   STRING; 198214.SF1578; -.
DR   EnsemblBacteria; AAN43166; AAN43166; SF1578.
DR   EnsemblBacteria; AAP17058; AAP17058; S1704.
DR   GeneID; 1023374; -.
DR   KEGG; sfl:SF1578; -.
DR   KEGG; sft:NCTC1_01711; -.
DR   KEGG; sfx:S1704; -.
DR   PATRIC; fig|198214.7.peg.1867; -.
DR   HOGENOM; CLU_057069_1_0_6; -.
DR   OrthoDB; 1560751at2; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; 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; Reference proteome; Schiff base; Transferase.
FT   CHAIN           1..256
FT                   /note="3-hydroxy-5-phosphonooxypentane-2,4-dione thiolase"
FT                   /id="PRO_0000351531"
FT   ACT_SITE        168
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P76143"
SQ   SEQUENCE   256 AA;  28044 MW;  72D58EC48CD261FB CRC64;
     MQSRLSWIFN PKTGKTVMLA FDHGYFQGPT IGLERIDINI APLFEHADVL MCTRGILRSV
     VPPATNKPVV LRASGANSIL AELSNEAVAL SMDDAVRLNS CAVAAQVYIG SEYEHQSIKN
     IIQLVDAGMK VGMPTMAVTG VGKDMVRDQR YFSLATRIAA EMGAQIIKTY YVEKGFERIV
     AGCPVPIVIA GGKKLPERET LEMCWQAIDQ GASGVDMGRN IFQSDHPVAM MKAVQAVVHH
     NETADRAYEL YLSEKQ